2IYV
Shikimate kinase from Mycobacterium tuberculosis in complex with ADP, open LID (conf. B)
Summary for 2IYV
| Entry DOI | 10.2210/pdb2iyv/pdb |
| Related | 1L4U 1L4Y 1U8A 1ZYU 2G1J 2G1K 2IYQ 2IYR 2IYS 2IYT 2IYU 2IYW 2IYX 2IYY 2IYZ |
| Descriptor | SHIKIMATE KINASE, ADENOSINE-5'-DIPHOSPHATE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | transferase, aromatic amino acid biosynthesis, p-loop kinase, metal- binding, shikimate kinase, shikimate pathway, nucleotide- binding, amino-acid biosynthesis, kinase, magnesium, atp-binding |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 20146.16 |
| Authors | Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D. (deposition date: 2006-07-22, release date: 2006-10-11, Last modification date: 2023-12-13) |
| Primary citation | Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D. Mechanism of Phosphoryl Transfer Catalyzed by Shikimate Kinase from Mycobacterium Tuberculosis. J.Mol.Biol., 364:411-, 2006 Cited by PubMed Abstract: The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate. PubMed: 17020768DOI: 10.1016/J.JMB.2006.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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