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| {{STRUCTURE_2pg7| PDB=2pg7 | SCENE= }} | | {{STRUCTURE_2pg7| PDB=2pg7 | SCENE= }} |
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| '''Crystal Structure of Human Microsomal P450 2A6 N297Q/I300V'''
| | ===Crystal Structure of Human Microsomal P450 2A6 N297Q/I300V=== |
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| ==Overview==
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| 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}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: P450]] | | [[Category: P450]] |
| [[Category: P450 2a6]] | | [[Category: P450 2a6]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:03:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:34:58 2008'' |
