1oxa: Difference between revisions
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==CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)== | ==CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)== | ||
<StructureSection load='1oxa' size='340' side='right' caption='[[1oxa]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1oxa' size='340' side='right'caption='[[1oxa]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oxa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXA FirstGlance]. <br> | <table><tr><td colspan='2'>[[1oxa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXA FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1oxa" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1oxa" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharopolyspora erythraea]] | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: Cupp-Vickery, J R]] | [[Category: Cupp-Vickery, J R]] | ||
[[Category: Poulos, T L]] | [[Category: Poulos, T L]] | ||
Revision as of 13:23, 27 November 2019
CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)
Structural highlights
Function[CPXJ_SACEN] Catalyzes the NADPH-dependent conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several alpha-helices. The largest difference occurs in the B' helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction. Structure of cytochrome P450eryF involved in erythromycin biosynthesis.,Cupp-Vickery JR, Poulos TL Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:7749919[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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