2iyo: Difference between revisions

Revision as of 18:25, 27 July 2008

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File:2iyo.png

Template:STRUCTURE 2iyo

STRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITIONSTRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITION

Template:ABSTRACT PUBMED 17222187

About this StructureAbout this Structure

2IYO is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates., Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN, FEBS J. 2007 Jan;274(1):275-86. PMID:17222187

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

OCA

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-'''STRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITION'''
+===STRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITION===
-==Overview==
+<!--
-Crystal structures of recombinant Lactococcus lactis 6-phosphogluconate dehydrogenase (LlPDH) in complex with substrate, cofactor, product and inhibitors have been determined. LlPDH shares significant sequence identity with the enzymes from sheep liver and the protozoan parasite Trypanosoma brucei for which structures have been reported. Comparisons indicate that the key residues in the active site are highly conserved, as are the interactions with the cofactor and the product ribulose 5-phosphate. However, there are differences in the conformation of the substrate 6-phosphogluconate which may reflect distinct states relevant to catalysis. Analysis of the complex formed with the potent inhibitor 4-phospho-d-erythronohydroxamic acid, suggests that this molecule does indeed mimic the high-energy intermediate state that it was designed to. The analysis also identified, as a contaminant by-product of the inhibitor synthesis, 4-phospho-d-erythronamide, which binds in similar fashion. LlPDH can now serve as a model system for structure-based inhibitor design targeting the enzyme from Trypanosoma species.
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 [[Category: Oxidoreductase,gluconate utilization]]
 [[Category: Pentose shunt]]
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