RECcheY-homologous receiver domain
|SMART accession number:||SM00448|
|Description:||CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.|
|Interpro abstract (IPR001789):|
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [(PUBMED:16176121)]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [(PUBMED:18076326)]. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more [(PUBMED:12372152)]. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) [(PUBMED:10966457)]. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.
A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [(PUBMED:11934609), (PUBMED:11489844)].
Bipartite response regulator proteins are involved in a two-component signal transduction system in bacteria, and certain eukaryotes like protozoa, that functions to detect and respond to environmental changes [(PUBMED:7699720)]. These systems have been detected during host invasion, drug resistance, motility, phosphate uptake, osmoregulation, and nitrogen fixation, amongst others [(PUBMED:12015152)]. The two-component system consists of a histidine protein kinase environmental sensor that phosphorylates the receiver domain of a response regulator protein; phosphorylation induces a conformational change in the response regulator, which activates the effector domain, triggering the cellular response [(PUBMED:10966457)]. The domains of the two-component proteins are highly modular, but the core structures and activities are maintained.
The response regulators act as phosphorylation-activated switches to affect a cellular response, usually by transcriptional regulation. Most of these proteins consist of two domains, an N-terminal response regulator receiver domain, and a variable C-terminal effector domain with DNA-binding activity. This entry represents the response regulator receiver domain, which belongs to the CheY family, and receives the signal from the sensor partner in the two-component system.
|GO process:||regulation of transcription, DNA-dependent (GO:0006355), two-component signal transduction system (phosphorelay) (GO:0000160)|
|GO function:||two-component response regulator activity (GO:0000156)|
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- Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a REC domain in a specific node, click on it.
This tree shows only several representative species. The complete taxonomic breakdown of all proteins with REC domain is also avaliable.
- Cellular role (predicted cellular role)
Cellular role: signalling
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Pao GM, SaierMHJ r
- Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution.
- J Mol Evol. 1995; 40: 136-54
- Display abstract
Response regulators of bacterial sensory transduction systems generally consist of receiver module domains covalently linked to effector domains. The effector domains include DNA binding and/or catalytic units that are regulated by sensor kinase-catalyzed aspartyl phosphorylation within their receiver modules. Most receiver modules are associated with three distinct families of DNA binding domains, but some are associated with other types of DNA binding domains, with methylated chemotaxis protein (MCP) demethylases, or with sensor kinases. A few exist as independent entities which regulate their target systems by noncovalent interactions. In this study the molecular phylogenies of the receiver modules and effector domains of 49 fully sequenced response regulators and their homologues were determined. The three major, evolutionarily distinct, DNA binding domains found in response regulators were evaluated for their phylogenetic relatedness, and the phylogenetic trees obtained for these domains were compared with those for the receiver modules. Members of one family (family 1) of DNA binding domains are linked to large ATPase domains which usually function cooperatively in the activation of E. coli sigma 54-dependent promoters or their equivalents in other bacteria. Members of a second family (family 2) always function in conjunction with the E. coli sigma 70 or its equivalent in other bacteria. A third family of DNA binding domains (family 3) functions by an uncharacterized mechanism involving more than one sigma factor. These three domain families utilize distinct helix-turn-helix motifs for DNA binding. The phylogenetic tree of the receiver modules revealed three major and several minor clusters of these domains. The three major receiver module clusters (clusters 1, 2, and 3) generally function with the three major families of DNA binding domains (families 1, 2, and 3, respectively) to comprise three classes of response regulators (classes 1, 2, and 3), although several exceptions exist. The minor clusters of receiver modules were usually, but not always, associated with other types of effector domains. Finally, several receiver modules did not fit into a cluster. It was concluded that receiver modules usually diverged from common ancestral protein domains together with the corresponding effector domains, although domain shuffling, due to intragenic splicing and fusion, must have occurred during the evolution of some of these proteins. Multiple sequence alignments of the 49 receiver modules and their various types of effector domains, together with other homologous domains, allowed definition of regions of striking sequence similarity and degrees of conservation of specific residues. Sequence data were correlated with structure/function when such information was available.(ABSTRACT TRUNCATED AT 250 WORDS)
- Volz K
- Structural conservation in the CheY superfamily.
- Biochemistry. 1993; 32: 11741-53
- Stock JB, Stock AM, Mottonen JM
- Signal transduction in bacteria.
- Nature. 1990; 344: 395-400
- Display abstract
Cells display a remarkable ability to respond to small fluctuations in their surroundings. In simple microbial systems, information from sensory receptors feeds into a circuitry of regulatory proteins that transfer high energy phosphoryl groups from histidine to aspartate side chains. This phosphotransfer network couples environmental signals to an array of response elements that control cell motility and regulate gene expression.
- Stock AM, Mottonen JM, Stock JB, Schutt CE
- Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis.
- Nature. 1989; 337: 745-9
- Display abstract
Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.
- Drlica K, Rouviere-Yaniv J
- Histonelike proteins of bacteria.
- Microbiol Rev. 1987; 51: 301-19
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 77.92 map02020 Two-component system - General 16.71 map02030 Bacterial chemotaxis - General 4.51 map03090 Type II secretion system 0.24 map00240 Pyrimidine metabolism 0.14 map00230 Purine metabolism 0.05 map00620 Pyruvate metabolism 0.05 map04910 Insulin signaling pathway 0.05 map00010 Glycolysis / Gluconeogenesis 0.05 map00710 Carbon fixation 0.05 map04930 Type II diabetes mellitus 0.05 map00540 Lipopolysaccharide biosynthesis 0.02 map00260 Glycine, serine and threonine metabolism 0.02 map00680 Methane metabolism 0.02 map00562 Inositol phosphate metabolism 0.02 map00190 Oxidative phosphorylation 0.02 map00630 Glyoxylate and dicarboxylate metabolism 0.02 map02010 ABC transporters - General 0.02 map00632 Benzoate degradation via CoA ligation 0.02 map00633 Trinitrotoluene degradation
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with REC domain which could be assigned to a KEGG orthologous group, and not all proteins containing REC domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of REC domains in PDB
PDB code Main view Title 1a04 The structure of the nitrate/nitrite response regulator protein narl in the monoclinic c2 crystal form 1a0o Chey-binding domain of chea in complex with chey 1a2o Structural basis for methylesterase cheb regulation by a phosphorylation-activated domain 1ab5 Structure of chey mutant f14n, v21t 1ab6 Structure of chey mutant f14n, v86t 1b00 Phob receiver domain from escherichia coli 1bdj Complex structure of hpt domain and chey 1c4w 1.9 a structure of a-thiophosphonate modified chey d57c 1cey Assignments, secondary structure, global fold, and dynamics of chemotaxis y protein using three-and four-dimensional heteronuclear (13c,15n) nmr spectroscopy 1chn Magnesium binding to the bacterial chemotaxis protein chey results in large conformational changes involving its functional surface 1cye Three dimensional structure of chemotactic che y protein in aqueous solution by nuclear magnetic resonance methods 1d4z Crystal structure of chey-95iv, a hyperactive chey mutant 1d5w Phosphorylated fixj receiver domain 1dbw Crystal structure of fixj-n 1dc7 Structure of a transiently phosphorylated "switch" in bacterial signal transduction 1dc8 Structure of a transiently phosphorylated "switch" in bacterial signal transduction 1dcf Crystal structure of the receiver domain of the ethylene receptor of arabidopsis thaliana 1dck Structure of unphosphorylated fixj-n complexed with mn2+ 1dcm Structure of unphosphorylated fixj-n with an atypical conformer (monomer a) 1djm Solution structure of bef3-activated chey from escherichia coli 1dz3 Domain-swapping in the sporulation response regulator spo0a 1e6k Two-component signal transduction system d12a mutant of chey 1e6l Two-component signal transduction system d13a mutant of chey 1e6m Two-component signal transduction system d57a mutant of chey 1eay Chey-binding (p2) domain of chea in complex with chey from escherichia coli 1ehc Structure of signal transduction protein chey 1f4v Crystal structure of activated chey bound to the n-terminus of flim 1f51 A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in singal transduction 1ffg Chey-binding domain of chea in complex with chey at 2.1 a resolution 1ffs Chey-binding domain of chea in complex with chey from crystals soaked in acetyl phosphate 1ffw Chey-binding domain of chea in complex with chey with a bound imido diphosphate 1fqw Crystal structure of activated chey 1fsp Nmr solution structure of bacillus subtilis spo0f protein, structures 1hey Investigating the structural determinants of the p21-like triphosphate and mg2+ binding site 1i3c Response regulator for cyanobacterial phytochrome, rcp1 1j56 Minimized average structure of beryllofluoride-activated ntrc receiver domain: model structure incorporating active site contacts 1jbe 1.08 a structure of apo-chey reveals meta-active conformation 1jlk Crystal structure of the mn(2+)-bound form of response regulator rcp1 1k66 Crystal structure of the cyanobacterial phytochrome response regulator, rcpb 1k68 Crystal structure of the phosphorylated cyanobacterial phytochrome response regulator rcpa 1kgs Crystal structure at 1.50 a of an ompr/phob homolog from thermotoga maritima 1kmi Crystal structure of an e.coli chemotaxis protein, chez 1krw Solution structure and backbone dynamics of beryllofluoride- activated ntrc receiver domain 1krx Solution structure of beryllofluoride-activated ntrc receiver domain: model structures incorporating active site contacts 1l5y Crystal structure of mg2+ / bef3-bound receiver domain of sinorhizobium meliloti dctd 1l5z Crystal structure of the e121k substitution of the receiver domain of sinorhizobium meliloti dctd 1m5t Crystal structure of the response regulator divk 1m5u Crystal structure of the response regulator divk. structure at ph 8.0 in the apo-form 1mav Crystal structure of the response regulator divk at ph 6.0 in complex with mn2+ 1mb0 Crystal structure of the response regulator divk at ph 8.0 in complex with mn2+ 1mb3 Crystal structure of the response regulator divk at ph 8.5 in complex with mg2+ 1mih A role for chey glu 89 in chez-mediated dephosphorylation of the e. coli chemotaxis response regulator chey 1mvo Crystal structure of the phop receiver domain from bacillus subtilis 1nat Crystal structure of spoof from bacillus subtilis 1ntr Solution structure of the n-terminal receiver domain of ntrc 1nxo Micarec ph7.0 1nxp Micarec ph4.5 1nxs Micarec ph4.9 1nxt Micarec ph 4.0 1nxv Micarec ph 4.2 1nxw Micarec ph 5.1 1nxx Micarec ph 5.5 1ny5 Crystal structure of sigm54 activator (aaa+ atpase) in the inactive state 1oxb Complex between ypd1 and sln1 response regulator domain in space group p2(1)2(1)2(1) 1oxk Complex between ypd1 and sln1 response regulator domain in space group p3(2) 1p2f Crystal structure analysis of response regulator drrb, a thermotoga maritima ompr/phob homolog 1p6q Nmr structure of the response regulator chey2 from sinorhizobium meliloti, complexed with mg++ 1p6u Nmr structure of the bef3-activated structure of the response regulator chey2-mg2+ from sinorhizobium meliloti 1pey Crystal structure of the response regulator spo0f complexed with mn2+ 1pux Nmr solution structure of bef3-activated spo0f, 20 conformers 1qkk Crystal structure of the receiver domain and linker region of dctd from sinorhizobium meliloti 1qmp Phosphorylated aspartate in the crystal structure of the sporulation response regulator, spo0a 1rnl The nitrate/nitrite response regulator protein narl from narl 1s8n Crystal structure of rv1626 from mycobacterium tuberculosis 1sd5 Crystal structure of rv1626 1srr Crystal structure of a phosphatase resistant mutant of sporulation response regulator spo0f from bacillus subtilis 1tmy Chey from thermotoga maritima (apo-i) 1u0s Chemotaxis kinase chea p2 domain in complex with response regulator chey from the thermophile thermotoga maritima 1u8t Crystal structure of chey d13k y106w alone and in complex with a flim peptide 1udr Chey mutant with lys 91 replaced by asp, lys 92 replaced by ala, ile 96 replaced by lys and ala 98 replaced by leu (stabilizing mutations in helix 4) 1vlz Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 angstrom structure of a threonine to isoleucine mutant at position 87 of chey 1w25 Response regulator pled in complex with c-digmp 1xhe Crystal structure of the receiver domain of redox response regulator arca 1xhf Crystal structure of the bef3-activated receiver domain of redox response regulator arca 1yio Crystallographic structure of response regulator styr from pseudomonas fluorescens 1ymu Signal transduction protein chey mutant with met 17 replaced by gly (m17g) 1ymv Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by gly, and met 17 replaced by gly 1ys6 Crystal structure of the response regulatory protein prra from mycobacterium tuberculosis 1ys7 Crystal structure of the response regulator protein prra comlexed with mg2+ 1zdm Crystal structure of activated chey bound to xe 1zes Bef3- activated phob receiver domain 1zgz Crystal structure of the receiver domain of tmao respiratory system response regulator torr 1zh2 Crystal structure of the calcium-bound receiver domain of kdp potassium transport system response regulator kdpe 1zh4 Crystal structure of the mg+2/bef3-bound receiver domain of kdp potassium transport system response regulator kdpe 1zit Structure of the receiver domain of ntrc4 from aquifex aeolicus 1zn2 Low resolution structure of response regulator styr 1zy2 Crystal structure of the phosphorylated receiver domain of the transcription regulator ntrc1 from aquifex aeolicus 2a9o Crystal structures of an activated yycf homologue, the essential response regulator from s.pneumoniae in complex with bef3 and the effect of ph on bef3 binding, possible phosphate in the active site 2a9p Medium resolution bef3 bound rr02-rec 2a9q Low resolution structure rr02-rec on bef3 bound 2a9r Rr02-rec phosphate in the active site 2ayx Solution structure of the e.coli rcsc c-terminus (residues 700-949) containing linker region and phosphoreceiver domain 2ayz Solution structure of the e.coli rcsc c-terminus (residues 817-949) containing phosphoreceiver domain 2b1j Crystal structure of unphosphorylated chey bound to the n- terminus of flim 2b4a Crystal structure of bh3024 protein (10175646) from bacillus halodurans at 2.42 a resolution 2che Structure of the mg2+-bound form of chey and mechanism of phosphoryl transfer in bacterial chemotaxis 2chf Structure of the mg2+-bound form of chey and the mechanism of phosphoryl transfer in bacterial chemotaxis 2chy Three-dimensional structure of chey, the response regulator of bacterial chemotaxis 2fka Crystal structure of mg(2+) and bef(3)(-)-bound chey in complex with chez(200-214) solved from a f432 crystal grown in caps (ph 10.5) 2flk Crystal structure of chey in complex with chez(200-214) solved from a f432 crystal grown in caps (ph 10.5) 2flw Crystal structure of mg2+ and bef3- ound chey in complex with chez 200-214 solved from a f432 crystal grown in hepes (ph 7.5) 2fmf Crystal structure of chey in complex with chez 200-214 solved from a f432 crystal grown in hepes (ph 7.5) 2fmh Crystal structure of mg2+ and bef3- bound chey in complex with chez 200-214 solved from a f432 crystal grown in tris (ph 8.4) 2fmi Crystal structure of chey in complex with chez 200-214 solved from a f432 crystal grown in tris (ph 8.4) 2fmk Crystal structure of mg2+ and bef3- bound chey in complex with chez 200-214 solved from a p2(1)2(1)2 crystal grown in mes (ph 6.0) 2fsp Nmr solution structure of bacillus subtilis spo0f protein, minimized average structure 2ftk Berylloflouride spo0f complex with spo0b 2gkg Receiver domain from myxococcus xanthus social motility protein frzs 2gwr Crystal structure of the response regulator protein mtra from mycobacterium tuberculosis 2hqo Structure of a atypical orphan response regulator protein revealed a new phosphorylation-independent regulatory mechanism 2hqr Structure of a atypical orphan response regulator protein revealed a new phosphorylation-independent regulatory mechanism 2i6f Receiver domain from myxococcus xanthus social motility protein frzs 2id7 1.75 a structure of t87i phosphono-chey 2id9 1.85 a structure of t87i/y106w phosphono-chey 2idm 2.00 a structure of t87i/y106w phosphono-chey 2iyn The co-factor-induced pre-active conformation in phob 2j48 Nmr structure of the pseudo-receiver domain of the cika protein. 2jb9 Phob response regulator receiver domain constitutively- active double mutant d10a and d53e. 2jba Phob response regulator receiver domain constitutively- active double mutant d53a and y102c. 2jk1 Crystal structure of the wild-type hupr receiver domain 2jrl Solution structure of the beryllofluoride-activated ntrc4 receiver domain dimer 2jvi Nmr solution structure of the hyper-sporulation response regulator spo0f mutant h101a from bacillus subtilis 2jvj Nmr solution structure of the hyper-sporulation response regulator spo0f mutant i90a from bacillus subtilis 2jvk Nmr solution structure of the hyper-sporulation response regulator spo0f mutant l66a from bacillus subtilis 2nt3 Receiver domain from myxococcus xanthus social motility protein frzs (y102a mutant) 2nt4 Receiver domain from myxococcus xanthus social motility protein frzs (h92f mutant) 2oqr The structure of the response regulator regx3 from mycobacterium tuberculosis 2pkx E.coli response regulator phop receiver domain 2pl1 Berrylium fluoride activated receiver domain of e.coli phop 2pl9 Crystal structure of chey-mg(2+)-bef(3)(-) in complex with chez(c19) peptide solved from a p2(1)2(1)2 crystal 2pln Crystal structure analysis of hp1043, an orphan resonse regulator of h. pylori 2pmc Crystal structure of chey-mg(2+) in complex with chez(c15) peptide solved from a p1 crystal 2qr3 Crystal structure of the n-terminal signal receiver domain of two-component system response regulator from bacteroides fragilis 2qsj Crystal structure of a luxr family dna-binding response regulator from silicibacter pomeroyi 2qv0 Crystal structure of the response regulatory domain of protein mrke from klebsiella pneumoniae 2qvg The crystal structure of a two-component response regulator from legionella pneumophila 2qxy Crystal structure of a response regulator from thermotoga maritima 2qzj Crystal structure of a two-component response regulator from clostridium difficile 2r25 Complex of ypd1 and sln1-r1 with bound mg2+ and bef3- 2rdm Crystal structure of response regulator receiver protein from sinorhizobium medicae wsm419 2rjn Crystal structure of an uncharacterized protein q2bku2 from neptuniibacter caesariensis 2tmy Chey from thermotoga maritima (apo-ii) 2v0n Activated response regulator pled in complex with c-digmp and gtp-alpha-s 2vuh Crystal structure of the d55e mutant of the hupr receiver domain 2vui Crystal structure of the hupr receiver domain in inhibitory phospho-state 2zay Crystal structure of response regulator from desulfuromonas acetoxidans 2zwm Crystal structure of yycf receiver domain from bacillus subtilis 3a0r Crystal structure of histidine kinase thka (tm1359) in complex with response regulator protein trra (tm1360) 3a0u Crystal structure of response regulator protein trra (tm1360) from thermotoga maritima in complex with mg(2+)- bef (wild type) 3a10 Crystal structure of response regulator protein trra (tm1360) from thermotoga maritima in complex with mg(2+)- bef (semet, l89m) 3b2n Crystal structure of dna-binding response regulator, luxr family, from staphylococcus aureus 3bre Crystal structure of p.aeruginosa pa3702 3c3m Crystal structure of the n-terminal domain of response regulator receiver protein from methanoculleus marisnigri jr1 3c3w Crystal structure of the mycobacterium tuberculosis hypoxic response regulator dosr 3c97 Crystal structure of the response regulator receiver domain of a signal transduction histidine kinase from aspergillus oryzae 3cfy Crystal structure of signal receiver domain of putative luxo repressor protein from vibrio parahaemolyticus 3cg0 Crystal structure of signal receiver domain of modulated diguanylate cyclase from desulfovibrio desulfuricans g20, an example of alternate folding 3cg4 Crystal structure of response regulator receiver domain protein (chey-like) from methanospirillum hungatei jf-1 3chy Crystal structure of escherichia coli chey refined at 1.7- angstrom resolution 3cnb Crystal structure of signal receiver domain of dna binding response regulator protein (merr) from colwellia psychrerythraea 34h 3crn Crystal structure of response regulator receiver domain protein (chey-like) from methanospirillum hungatei jf-1 3cu5 Crystal structure of a two component transcriptional regulator arac from clostridium phytofermentans isdg 3cwo A beta/alpha-barrel built by the combination of fragments from different folds 3cz5 Crystal structure of two-component response regulator, luxr family, from aurantimonas sp. si85-9a1 3dge Structure of a histidine kinase-response regulator complex reveals insights into two-component signaling and a novel cis-autophosphorylation mechanism 3dgf Structure of a histidine kinase-response regulator complex reveals insights into two-component signaling and a novel cis-autophosphorylation mechanism 3dzd Crystal structure of sigma54 activator ntrc4 in the inactive state 3eod Crystal structure of n-terminal domain of e. coli rssb 3eq2 Structure of hexagonal crystal form of pseudomonas aeruginosa rssb 3eqz Crystal structure of a response regulator from colwellia psychrerythraea 3eul Structure of the signal receiver domain of the putative response regulator narl from mycobacterium tuberculosis 3f6c Crystal structure of n-terminal domain of positive transcription regulator evga from escherichia coli 3f7a Structure of orthorhombic crystal form of pseudomonas aeruginosa rssb 3f7n Crystal structure of chey triple mutant f14e, n59m, e89l complexed with bef3- and mn2+ 3fft Crystal structure of chey double mutant f14e, e89r complexed with bef3- and mn2+ 3ffw Crystal structure of chey triple mutant f14q, n59k, e89y complexed with bef3- and mn2+ 3ffx Crystal structure of chey triple mutant f14e, n59r, e89h complexed with bef3- and mn2+ 3fgz Crystal structure of chey triple mutant f14e, n59m, e89r complexed with bef3- and mn2+ 3gl9 The structure of a histidine kinase-response regulator complex sheds light into two-component signaling and reveals a novel cis autophosphorylation mechanism 3grc Crystal structure of a sensor protein from polaromonas sp. js666 3gt7 Crystal structure of signal receiver domain of signal transduction histidine kinase from syntrophus aciditrophicus 3h5i Crystal structure of the n-terminal domain of a response regulator/sensory box/ggdef 3-domain protein from carboxydothermus hydrogenoformans 3hdg Crystal structure of the n-terminal domain of an uncharacterized protein (ws1339) from wolinella succinogenes 3hdv Crystal structure of response regulator receiver protein from pseudomonas putida 3heb Crystal structure of response regulator receiver domain from rhodospirillum rubrum 3hv2 Crystal structure of signal receiver domain of hd domain- containing protein from pseudomonas fluorescens pf-5 3i42 Structure of response regulator receiver domain (chey-like) from methylobacillus flagellatus 3i5a Crystal structure of full-length wpsr from pseudomonas syringae 3ilh Crystal structure of two component response regulator from cytophaga hutchinsonii 3jte Crystal structure of response regulator receiver domain protein from clostridium thermocellum 3kcn The crystal structure of adenylate cyclase from rhodopirellula baltica 3kht Crystal structure of response regulator from hahella chejuensis 3tmy Chey from thermotoga maritima (mn-iii) 4tmy Chey from thermotoga maritima (mg-iv) 5chy Structure of chemotaxis protein chey 6chy Structure of chemotaxis protein chey
- Links (links to other resources describing this domain)
PFAM response_reg INTERPRO IPR001789