2iyz
From Proteopedia
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| - | [[Image:2iyz.gif|left|200px]]<br /> | + | [[Image:2iyz.gif|left|200px]]<br /><applet load="2iyz" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2iyz" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2iyz, resolution 2.30Å" /> | caption="2iyz, resolution 2.30Å" /> | ||
'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND ADP'''<br /> | '''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND ADP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with S3P and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] | + | 2IYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with S3P and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] Known structural/functional Site: <scene name='pdbsite=AC1:Adp Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IYZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:41:25 2007'' |
Revision as of 17:31, 18 December 2007
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND ADP
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
2IYZ is a Single protein structure of sequence from Mycobacterium tuberculosis with S3P and ADP as ligands. 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
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Categories: Mycobacterium tuberculosis | Shikimate kinase | Single protein | Bartunik, H.D. | Bourenkov, G.P. | Hartmann, M.D. | Oberschall, A. | Strizhov, N. | ADP | S3P | Amino-acid biosynthesis | Aromatic amino acid biosynthesis | Atp-binding | Kinase | Magnesium | Metal-binding | Nucleotide-binding | P-loop kinase | Shikimate pathway | Transferase
