2pg5
From Proteopedia
(New page: 200px<br /> <applet load="2pg5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pg5, resolution 1.950Å" /> '''Crystal Structure ...) |
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| - | [[Image:2pg5.gif|left|200px]]<br /> | + | [[Image:2pg5.gif|left|200px]]<br /><applet load="2pg5" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2pg5, resolution 1.950Å" /> | caption="2pg5, resolution 1.950Å" /> | ||
'''Crystal Structure of Human Microsomal P450 2A6 N297Q'''<br /> | '''Crystal Structure of Human Microsomal P450 2A6 N297Q'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http:// | + | 2PG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PG5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: p450 2a6]] | [[Category: p450 2a6]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:37:17 2008'' |
Revision as of 11:37, 23 January 2008
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Crystal Structure of Human Microsomal P450 2A6 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.
About this Structure
2PG5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Unspecific monooxygenase, with EC number 1.14.14.1 Full crystallographic information is available from OCA.
Reference
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 May 11;. PMID:17540336
Page seeded by OCA on Wed Jan 23 13:37:17 2008
Categories: Homo sapiens | Single protein | Unspecific monooxygenase | Hsu, M.H. | Johnson, E.F. | Sansen, S. | Stout, C.D. | EDO | HEM | Cyp2a6 | Drug metabolizing enzyme | Heme | Indole | Monooxygenases | Mutant | P450 | P450 2a6
