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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1oxa, resolution 2.1&Aring;" />
'''CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)'''<br />


==Overview==
==CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)==
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.
<StructureSection load='1oxa' size='340' side='right'caption='[[1oxa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oxa]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1OXA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEB:6-DEOXYERYTHRONOLIDE+B'>DEB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxa OCA], [https://pdbe.org/1oxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxa RCSB], [https://www.ebi.ac.uk/pdbsum/1oxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXJ_SACEN 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.<ref>PMID:1732208</ref> <ref>PMID:2011746</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oxa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
Structure of cytochrome P450eryF involved in erythromycin biosynthesis.,Cupp-Vickery JR, Poulos TL Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:7749919<ref>PMID:7749919</ref>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OXA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of cytochrome P450eryF involved in erythromycin biosynthesis., Cupp-Vickery JR, Poulos TL, Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7749919 7749919]
</div>
<div class="pdbe-citations 1oxa" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Single protein]]
[[Category: Cupp-Vickery JR]]
[[Category: Cupp-Vickery, J.R.]]
[[Category: Poulos TL]]
[[Category: Poulos, T.L.]]
[[Category: DEB]]
[[Category: HEM]]
[[Category: oxidoreductase (oxygenase)]]
 
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