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1oxa
From Proteopedia
(New page: 200px<br /><applet load="1oxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxa, resolution 2.1Å" /> '''CYTOCHROME P450 (DONO...) |
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| - | [[Image:1oxa.jpg|left|200px]]<br /><applet load="1oxa" size=" | + | [[Image:1oxa.jpg|left|200px]]<br /><applet load="1oxa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oxa, resolution 2.1Å" /> | caption="1oxa, resolution 2.1Å" /> | ||
'''CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)'''<br /> | '''CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide | + | Cytochrome 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea] with HEM and DEB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1OXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=DEB:'>DEB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXA OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Saccharopolyspora erythraea]] | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cupp-Vickery, J | + | [[Category: Cupp-Vickery, J R.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: DEB]] | [[Category: DEB]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: oxidoreductase (oxygenase)]] | [[Category: oxidoreductase (oxygenase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:42 2008'' |
Revision as of 12:22, 21 February 2008
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CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)
Overview
Cytochrome 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.
About this Structure
1OXA is a Single protein structure of sequence from Saccharopolyspora erythraea with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of cytochrome P450eryF involved in erythromycin biosynthesis., Cupp-Vickery JR, Poulos TL, Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:7749919
Page seeded by OCA on Thu Feb 21 14:22:42 2008
