2iyr: Difference between revisions
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[[Image:2iyr.gif|left|200px]]<br /><applet load="2iyr" size=" | [[Image:2iyr.gif|left|200px]]<br /><applet load="2iyr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2iyr, resolution 1.98Å" /> | caption="2iyr, resolution 1.98Å" /> | ||
'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE'''<br /> | '''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2IYR 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 SKM 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] Known structural/functional Site: <scene name='pdbsite=AC1:Skm Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 2IYR 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=SKM:'>SKM</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Skm+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 11:39, 3 February 2008
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SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE
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 identified a, synergic mechanism by which binding of the first substrate may enhance the, affinity for the second substrate.
About this StructureAbout 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.
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.
- SKM
- Amino-acid biosynthesis
- Aromatic amino acid biosynthesis
- Atp-binding
- Kinase
- Magnesium
- Metal-binding
- Nucleotide-binding
- P-loop kinase
- Shikimate pathway
- Transferase