1KOR
Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with inhibitors
Summary for 1KOR
| Entry DOI | 10.2210/pdb1kor/pdb |
| Related | 1KH1 1KH2 1KH3 |
| Descriptor | Argininosuccinate Synthetase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ARGININE, ... (5 entities in total) |
| Functional Keywords | ligase, riken structural genomics/proteomics initiative, rsgi, structural genomics |
| Biological source | Thermus thermophilus |
| Cellular location | Cytoplasm (Probable): P59846 |
| Total number of polymer chains | 4 |
| Total formula weight | 182701.94 |
| Authors | Goto, M.,Nakajima, Y.,Hirotsu, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-12-22, release date: 2002-04-03, Last modification date: 2024-12-25) |
| Primary citation | Goto, M.,Nakajima, Y.,Hirotsu, K. Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action. J.Biol.Chem., 277:15890-15896, 2002 Cited by PubMed Abstract: Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its free form, complexed with intact ATP, and complexed with an ATP analogue (adenylyl imidodiphosphate) and substrate analogues (arginine and succinate) have been determined at 2.3-, 2.3-, and 1.95-A resolution, respectively. The structure is essentially the same as that of the Escherichia coli argininosuccinate synthetase. The small domain has the same fold as that of a new family of "N-type" ATP pyrophosphatases with the P-loop specific for the pyrophosphate of ATP. However, the enzyme shows the P-loop specific for the gamma-phosphate of ATP. The structure of the complex form is quite similar to that of the native one, indicating that no conformational change occurs upon the binding of ATP and the substrate analogues. ATP and the substrate analogues are bound to the active site with their reaction sites close to one another and located in a geometrical orientation favorable to the catalytic action. The reaction mechanism so far proposed seems to be consistent with the locations of ATP and the substrate analogues. The reaction may proceed without the large conformational change of the enzyme proposed for the catalytic process. PubMed: 11844799DOI: 10.1074/jbc.M112430200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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