2iyy: Difference between revisions
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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 17:57:29 2008'' | ||
Revision as of 15:57, 21 February 2008
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND SO4
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
2IYY is a Single protein structure of sequence from Mycobacterium tuberculosis with SO4, PO4, MG, CL and S3P as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Known structural/functional Site: AC1. 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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Mycobacterium tuberculosis
- Shikimate kinase
- Single protein
- Bartunik, H D.
- Bourenkov, G P.
- Hartmann, M D.
- Oberschall, A.
- Strizhov, N.
- CL
- MG
- PO4
- S3P
- SO4
- Amino-acid biosynthesis
- Aromatic amino acid biosynthesis
- Atp-binding
- Kinase
- Magnesium
- Metal-binding
- Nucleotide-binding
- P-loop kinase
- Shikimate pathway
- Transferase
