2iyv
From Proteopedia
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| - | [[Image:2iyv.gif|left|200px]]<br /><applet load="2iyv" size=" | + | [[Image:2iyv.gif|left|200px]]<br /><applet load="2iyv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2iyv, resolution 1.35Å" /> | caption="2iyv, resolution 1.35Å" /> | ||
'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)'''<br /> | '''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IYV 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 CL 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:Cl Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2IYV 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 <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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:Cl+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:39:52 2008'' |
Revision as of 08:39, 3 February 2008
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)
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
2IYV is a Single protein structure of sequence from Mycobacterium tuberculosis with and 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 | CL | Amino-acid biosynthesis | Aromatic amino acid biosynthesis | Atp-binding | Kinase | Magnesium | Metal-binding | Nucleotide-binding | P-loop kinase | Shikimate pathway | Transferase
