2gew: Difference between revisions

Revision as of 14:57, 29 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:2gew.png

Template:STRUCTURE 2gew

Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)

Template:ABSTRACT PUBMED 16604066

About this StructureAbout this Structure

2GEW is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment., Lyubimov AY, Lario PI, Moustafa I, Vrielink A, Nat Chem Biol. 2006 May;2(5):259-64. Epub 2006 Apr 9. PMID:16604066

Page seeded by OCA on Tue Jul 29 14:57:15 2008

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

OCA

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-'''Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)'''
+===Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)===
-==Overview==
+<!--
-Hydrogen atoms are a vital component of enzyme structure and function. In recent years, atomic resolution crystallography (&gt;or=1.2 A) has been successfully used to investigate the role of the hydrogen atom in enzymatic catalysis. Here, atomic resolution crystallography was used to study the effect of pH on cholesterol oxidase from Streptomyces sp., a flavoenzyme oxidoreductase. Crystallographic observations of the anionic oxidized flavin cofactor at basic pH are consistent with the UV-visible absorption profile of the enzyme and readily explain the reversible pH-dependent loss of oxidation activity. Furthermore, a hydrogen atom, positioned at an unusually short distance from the main chain carbonyl oxygen of Met122 at high pH, was observed, suggesting a previously unknown mechanism of cofactor stabilization. This study shows how a redox active site responds to changes in the enzyme's environment and how these changes are able to influence the mechanism of enzymatic catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_16604066}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16604066 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16604066}}
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 [[Category: Oxidoreductase]]
 [[Category: Steroid metabolism]]
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