CPSase_L_D3Carbamoyl-phosphate synthetase large chain, oligomerisation domain |
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| SMART accession number: | SM01096
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| Description: |
Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. |
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| Interpro abstract (IPR005480): |
This entry represents the oligomerisation domain found in the large subunit of carbamoyl phosphate synthases as well as in certain other carboxy phosphate domain-containing enzymes. This domain forms a primarily alpha-helical fold [(PUBMED:10089390)].
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| Family alignment: |
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There are 3566
CPSase_L_D3 domains in 3566 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM
- The structure of carbamoyl phosphate synthetase determined to 2.1 Aresolution.
- Acta Crystallogr D Biol Crystallogr. 1999; 55: 8-24
- Display abstract
Carbamoyl phosphate synthetase catalyzes the formation of carbamoylphosphate from one molecule of bicarbonate, two molecules of Mg2+ATP andone molecule of glutamine or ammonia depending upon the particular form ofthe enzyme under investigation. As isolated from Escherichia coli, theenzyme is an alpha,beta-heterodimer consisting of a small subunit thathydrolyzes glutamine and a large subunit that catalyzes the two requiredphosphorylation events. Here the three-dimensional structure of carbamoylphosphate synthetase from E. coli refined to 2.1 A resolution with an Rfactor of 17.9% is described. The small subunit is distinctly bilobal witha catalytic triad (Cys269, His353 and Glu355) situated between the twostructural domains. As observed in those enzymes belonging to thealpha/beta-hydrolase family, the active-site nucleophile, Cys269, isperched at the top of a tight turn. The large subunit consists of fourstructural units: the carboxyphosphate synthetic component, theoligomerization domain, the carbamoyl phosphate synthetic component andthe allosteric domain. Both the carboxyphosphate and carbamoyl phosphatesynthetic components bind Mn2+ADP. In the carboxyphosphate syntheticcomponent, the two observed Mn2+ ions are both octahedrally coordinated byoxygen-containing ligands and are bridged by the carboxylate side chain ofGlu299. Glu215 plays a key allosteric role by coordinating to thephysiologically important potassium ion and hydrogen bonding to the ribosehydroxyl groups of ADP. In the carbamoyl phosphate synthetic component,the single observed Mn2+ ion is also octahedrally coordinated byoxygen-containing ligands and Glu761 plays a similar role to that ofGlu215. The carboxyphosphate and carbamoyl phosphate synthetic components,while topologically equivalent, are structurally different, as would beexpected in light of their separate biochemical functions.
- Structure (3D structures containing this domain)
3D Structures of CPSase_L_D3 domains in PDB
| PDB code | Main view | Title | | 1a9x |  | Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis |
| 1bxr |  | Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp |
| 1c30 |  | Crystal structure of carbamoyl phosphate synthetase: small subunit mutation c269s |
| 1c3o |  | Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine |
| 1ce8 |  | Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp |
| 1cs0 |  | Crystal structure of carbamoyl phosphate synthetase complexed at cys269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde |
| 1jdb |  | Carbamoyl phosphate synthetase from escherichia coli |
| 1kee |  | Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin |
| 1m6v |  | Crystal structure of the g359f (small subunit) point mutant of carbamoyl phosphate synthetase |
| 1t36 |  | Crystal structure of e. coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'- monophosphate |
- Links (links to other resources describing this domain)
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