2iyv: Difference between revisions

Revision as of 10:52, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2iyv.png

Template:STRUCTURE 2iyv

SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)

Template:ABSTRACT PUBMED 17020768

About this StructureAbout this Structure

2IYV is a Single protein structure of sequence from Mycobacterium tuberculosis. 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

Page seeded by OCA on Mon Jul 28 10:52:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH ADP, OPEN LID (CONF. B)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17020768}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17020768 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17020768}}
 ==About this Structure==
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 [[Category: Shikimate pathway]]
 [[Category: Transferase]]
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