2pg6: Difference between revisions

Revision as of 13:48, 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:2pg6.png

Template:STRUCTURE 2pg6

Crystal Structure of Human Microsomal P450 2A6 L240C/N297QCrystal Structure of Human Microsomal P450 2A6 L240C/N297Q

Template:ABSTRACT PUBMED 17540336

About this StructureAbout this Structure

2PG6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural insight into the altered substrate specificity of human cytochrome P450 2A6 mutants., Sansen S, Hsu MH, Stout CD, Johnson EF, Arch Biochem Biophys. 2007 Aug 15;464(2):197-206. Epub 2007 May 11. PMID:17540336

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-'''Crystal Structure of Human Microsomal P450 2A6 L240C/N297Q'''
+===Crystal Structure of Human Microsomal P450 2A6 L240C/N297Q===
-==Overview==
+<!--
-Human P450 2A6 displays a small active site that is well adapted for the oxidation of small planar substrates. Mutagenesis of CYP2A6 resulted in an increased catalytic efficiency for indole biotransformation to pigments and conferred a capacity to oxidize substituted indoles (Wu, Z.-L., Podust, L.M., Guengerich, F.P. J. Biol. Chem. 49 (2005) 41090-41100.). Here, we describe the structural basis that underlies the altered metabolic profile of three mutant enzymes, P450 2A6 N297Q, L240C/N297Q and N297Q/I300V. The Asn297 substitution abolishes a potential hydrogen bonding interaction with substrates in the active site, and replaces a structural water molecule between the helix B'-C region and helix I while maintaining structural hydrogen bonding interactions. The structures of the P450 2A6 N297Q/L240C and N297Q/I300V mutants provide clues as to how the protein can adapt to fit the larger substituted indoles in the active site, and enable a comparison with other P450 family 2 enzymes for which the residue at the equivalent position was seen to function in isozyme specificity, structural integrity and protein flexibility.
+The line below this paragraph, {{ABSTRACT_PUBMED_17540336}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17540336 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17540336}}
 ==About this Structure==
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 [[Category: P450]]
 [[Category: P450 2a6]]
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