3CSM
STRUCTURE OF YEAST CHORISMATE MUTASE WITH BOUND TRP AND AN ENDOOXABICYCLIC INHIBITOR
Summary for 3CSM
| Entry DOI | 10.2210/pdb3csm/pdb |
| Descriptor | CHORISMATE MUTASE, TRYPTOPHAN, 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID (3 entities in total) |
| Functional Keywords | chorismate pyruvatemutase, allosteric protein, complex (isomerase-peptide), transition state analog, complex (isomerase-peptide) complex, complex (isomerase/peptide) |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 60781.82 |
| Authors | Straeter, N.,Schnappauf, G.,Braus, G.,Lipscomb, W.N. (deposition date: 1997-07-10, release date: 1998-01-14, Last modification date: 2024-05-22) |
| Primary citation | Strater, N.,Schnappauf, G.,Braus, G.,Lipscomb, W.N. Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Structure, 5:1437-1452, 1997 Cited by PubMed Abstract: Chorismate mutase (CM) catalyzes the Claisen rearrangement of chorismate to prephenate, notably the only known enzymatically catalyzed pericyclic reaction in primary metabolism. Structures of the enzyme in complex with an endo-oxabicyclic transition state analogue inhibitor, previously determined for Bacillus subtilis and Escherichia coli CM, provide structural insight into the enzyme mechanism. In contrast to these bacterial CMs, yeast CM is allosterically regulated in two ways: activation by tryptophan and inhibition by tyrosine. Yeast CM exists in two allosteric states, R (active) and t (inactive). PubMed: 9384560DOI: 10.1016/S0969-2126(97)00294-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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