1ZA2
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution
Summary for 1ZA2
| Entry DOI | 10.2210/pdb1za2/pdb |
| Related | 1TU0 1ZA1 |
| Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | ordered substrate binding, cooperativity, transferase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 104645.66 |
| Authors | Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R. (deposition date: 2005-04-05, release date: 2005-06-07, Last modification date: 2023-08-23) |
| Primary citation | Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R. Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Proc.Natl.Acad.Sci.Usa, 102:8881-8886, 2005 Cited by PubMed Abstract: X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity. PubMed: 15951418DOI: 10.1073/pnas.0503742102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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