2iyt: Difference between revisions
New page: left|200px<br /> <applet load="2iyt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iyt, resolution 1.47Å" /> '''SHIKIMATE KINASE FR... |
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==About this Structure== | ==About this Structure== | ||
2IYT 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 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IYT OCA]]. | 2IYT 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 as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IYT OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17020768 17020768] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17020768 17020768] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Shikimate kinase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bartunik, H.D.]] | [[Category: Bartunik, H.D.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 13:44, 30 October 2007
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2IYT is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with CL as [ligand]. Active as [Shikimate kinase], with EC number [2.7.1.71]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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
- Amino-acid biosynthesis
- Aromatic amino acid biosynthesis
- Atp-binding
- Kinase
- Magnesium
- Metal-binding
- Nucleotide-binding
- P-loop kinase
- Shikimate pathway
- Transferase