Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Parraga G et al.
- Zinc-dependent structure of a single-finger domain of yeast ADR1.
- Science. 1988; 241: 1489-92
- Display abstract
In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an indepe
ZnF_CDGSHCDGSH-type zinc finger. Function unknown.
SMART accession number: SM00704 Description: - Interpro abstract (IPR006622):
This entry represents iron-sulphur domain containing proteins that have a CDGSH sequence motif (although the Ser residue can also be an Ala or Thr), and is found in proteins from a wide range of organisms with the exception of fungi. The CDGSH-type domain binds a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family [(PUBMED:17376863)].
CDGSH-type domains are found in mitoNEET, an iron-containing integral protein of the outer mitochondrian membrane (OMM). MitoNEET forms a dimeric structure with a NEET fold, and contains two domains: a beta-cap region and a cluster-binding domain that coordinated two acid-labile 2Fe-2S clusters (one bound to each protomer) [(PUBMED:17766440)]. The CDGSH iron-sulphur domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, (IPR019610) [(PUBMED:17584744), (PUBMED:17766440)]. The whole protein regulates oxidative capacity and may function in electron transfer, for instance in redox reactions with metabolic intermediates, cofactors and/or proteins localized at the OMM.
GO component: intracellular membrane-bounded organelle (GO:0043231) GO function: 2 iron, 2 sulfur cluster binding (GO:0051537) Family alignment:
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing ZnF_CDGSH domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with ZnF_CDGSH domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing ZnF_CDGSH domain in the selected taxonomic class.
- Metabolism (metabolic pathways involving proteins which contain this domain)
Click the image to view the interactive version of the map in iPath
% proteins involved KEGG pathway ID Description 40.00 map00251 Glutamate metabolism 40.00 map00910 Nitrogen metabolism 20.00 map00272 Cysteine metabolism
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 ZnF_CDGSH domain which could be assigned to a KEGG orthologous group, and not all proteins containing ZnF_CDGSH 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 ZnF_CDGSH domains in PDB
PDB code Main view Title 2qd0 Crystal structure of mitoNEET 2qh7 MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone 2r13 Crystal structure of human mitoNEET reveals a novel [2Fe-2S] cluster coordination 3ew0 The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain 3fnv Crystal Structure of Miner1: The Redox-active 2Fe-2S Protein Causative in Wolfram Syndrome 2 3lpq Human MitoNEET with 2Fe-2S Coordinating Ligand His 87 Replaced With Cys 3ree Crystal structure of mitoNEET 4ezf The Crystal Structure of a Human MitoNEET mutant with an Ala inserted between Asp 67 and Lys 68 4f1e The Crystal Structure of a Human MitoNEET mutant with Asp 67 replaced by a Gly 4f28 The Crystal Structure of a Human MitoNEET mutant with Met 62 Replaced by a Gly 4f2c The Crystal Structure of a Human MitoNEET double mutant in which Gly 66 are Asp 67 are both Replaced with Ala Residues
- Links (links to other resources describing this domain)