2iyr
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structural mechanism of the catalytic functioning of shikimate kinase | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Shikimate kinase]] | [[Category: Shikimate kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bartunik, H | + | [[Category: Bartunik, H D.]] |
| - | [[Category: Bourenkov, G | + | [[Category: Bourenkov, G P.]] |
| - | [[Category: Hartmann, M | + | [[Category: Hartmann, M D.]] |
[[Category: Oberschall, A.]] | [[Category: Oberschall, A.]] | ||
[[Category: Strizhov, N.]] | [[Category: Strizhov, N.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:27 2008'' |
Revision as of 15:57, 21 February 2008
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE
Overview
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.
About this Structure
2IYR is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Shikimate kinase, with EC number 2.7.1.71 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis., Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD, J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768
Page seeded by OCA on Thu Feb 21 17:57:27 2008
Categories: Mycobacterium tuberculosis | Shikimate kinase | Single protein | Bartunik, H D. | Bourenkov, G P. | Hartmann, M D. | Oberschall, A. | Strizhov, N. | SKM | Amino-acid biosynthesis | Aromatic amino acid biosynthesis | Atp-binding | Kinase | Magnesium | Metal-binding | Nucleotide-binding | P-loop kinase | Shikimate pathway | Transferase
