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{{Structure
==Crystal Structure of OxyC a Cytochrome P450 Implicated in an Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.==
|PDB= 1ued |SIZE=350|CAPTION= <scene name='initialview01'>1ued</scene>, resolution 1.90&Aring;
<StructureSection load='1ued' size='340' side='right'caption='[[1ued]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>
<table><tr><td colspan='2'>[[1ued]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UED FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ued FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ued OCA], [https://pdbe.org/1ued PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ued RCSB], [https://www.ebi.ac.uk/pdbsum/1ued PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ued ProSAT]</span></td></tr>
|RELATEDENTRY=[[1lfk|1LFK]], [[1lg9|1LG9]], [[1lgf|1LGF]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ued FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ued OCA], [http://www.ebi.ac.uk/pdbsum/1ued PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ued RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/C5C4_AMYOR C5C4_AMYOR] Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin.
== 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/ue/1ued_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ued ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gene inactivation studies point to the involvement of OxyC in catalyzing the last oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. Presently, the substrate and exact timing of the OxyC reaction are unknown. The substrate might be the bicyclic heptapeptide or a thioester derivative bound to a protein carrier domain. OxyC from the vancomycin producer Amycolatopsis orientalis was produced in Escherichia coli and crystallized, and its structure was determined to 1.9 A resolution. OxyC gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite the CO-ligated form gave a 450-nm peak in a UV-difference spectrum. The addition of vancomycin aglycone to OxyC produced type I changes to the UV spectrum. OxyC exhibits the typical P450-fold, with the Cys ligand loop containing the signature sequence FGHGX-HXCLG and Cys-356 being the proximal axial thiolate ligand of the heme iron. The observation of a water molecule bound to the heme iron is consistent with the UV-visible spectra of OxyC indicating a low spin heme. A polyethylene glycol molecule occupying the active site might mimic the bicyclic heptapeptide substrate. Analysis of the structure of Oxy-proteins and other P450s indicates regions that might be involved in binding of the redox partner and possibly the protein carrier domain.


'''Crystal Structure of OxyC a Cytochrome P450 Implicated in an Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.'''
Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis.,Pylypenko O, Vitali F, Zerbe K, Robinson JA, Schlichting I J Biol Chem. 2003 Nov 21;278(47):46727-33. Epub 2003 Jul 29. PMID:12888556<ref>PMID:12888556</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ued" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Gene inactivation studies point to the involvement of OxyC in catalyzing the last oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. Presently, the substrate and exact timing of the OxyC reaction are unknown. The substrate might be the bicyclic heptapeptide or a thioester derivative bound to a protein carrier domain. OxyC from the vancomycin producer Amycolatopsis orientalis was produced in Escherichia coli and crystallized, and its structure was determined to 1.9 A resolution. OxyC gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite the CO-ligated form gave a 450-nm peak in a UV-difference spectrum. The addition of vancomycin aglycone to OxyC produced type I changes to the UV spectrum. OxyC exhibits the typical P450-fold, with the Cys ligand loop containing the signature sequence FGHGX-HXCLG and Cys-356 being the proximal axial thiolate ligand of the heme iron. The observation of a water molecule bound to the heme iron is consistent with the UV-visible spectra of OxyC indicating a low spin heme. A polyethylene glycol molecule occupying the active site might mimic the bicyclic heptapeptide substrate. Analysis of the structure of Oxy-proteins and other P450s indicates regions that might be involved in binding of the redox partner and possibly the protein carrier domain.
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 
== References ==
==About this Structure==
<references/>
1UED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UED OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis., Pylypenko O, Vitali F, Zerbe K, Robinson JA, Schlichting I, J Biol Chem. 2003 Nov 21;278(47):46727-33. Epub 2003 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12888556 12888556]
[[Category: Amycolatopsis orientalis]]
[[Category: Amycolatopsis orientalis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Pylypenko, O.]]
[[Category: Pylypenko O]]
[[Category: Robinson, J A.]]
[[Category: Robinson JA]]
[[Category: Schlichting, I.]]
[[Category: Schlichting I]]
[[Category: Vitali, F.]]
[[Category: Vitali F]]
[[Category: Zerbe, K.]]
[[Category: Zerbe K]]
[[Category: cytochrome p450 vancomycin biosynthesis]]
 
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