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[[Image:1lfk.gif|left|200px]]


{{Structure
==Crystal structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin Biosynthesis==
|PDB= 1lfk |SIZE=350|CAPTION= <scene name='initialview01'>1lfk</scene>, resolution 1.70&Aring;
<StructureSection load='1lfk' size='340' side='right'caption='[[1lfk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
<table><tr><td colspan='2'>[[1lfk]] is a 1 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=1LFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LFK 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]] 1.7&#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></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=1lfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfk OCA], [https://pdbe.org/1lfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lfk RCSB], [https://www.ebi.ac.uk/pdbsum/1lfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfk ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfk OCA], [http://www.ebi.ac.uk/pdbsum/1lfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lfk RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/C5B3_AMYOR C5B3_AMYOR]
== 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/lf/1lfk_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=1lfk ConSurf].
<div style="clear:both"></div>


'''Crystal structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin Biosynthesis'''
==See Also==
 
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Gene-inactivation studies point to the involvement of OxyB in catalyzing the first oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. The oxyB gene has been cloned and sequenced from the vancomycin producer Amycolatopsis orientalis, and the hemoprotein has been produced in Escherichia coli, crystallized, and its structure determined to 1.7-A resolution. OxyB gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite or by spinach ferredoxin and ferredoxin reductase, the CO-ligated form gave a 450-nm peak in a UV-difference spectrum. Addition of putative heptapeptide substrates to resting OxyB produced type I changes to the UV spectrum, but no turnover was observed in the presence of ferredoxin and ferredoxin reductase, showing that either the peptides or the reduction system, or both, are insufficient to support a full catalytic cycle. OxyB exhibits the typical P450-fold, with helix L containing the signature sequence FGHGXHXCLG and Cys(347) being the proximal axial thiolate ligand of the heme iron. The structural similarity of OxyB is highest to P450nor, P450terp, CYP119, and P450eryF. In OxyB, the F and G helices are rotated out of the active site compared with P450nor, resulting in a much more open active site, consistent with the larger size of the presumed heptapeptide substrate.
 
==About this Structure==
1LFK 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=1LFK OCA].
 
==Reference==
Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis., Zerbe K, Pylypenko O, Vitali F, Zhang W, Rouset S, Heck M, Vrijbloed JW, Bischoff D, Bister B, Sussmuth RD, Pelzer S, Wohlleben W, Robinson JA, Schlichting I, J Biol Chem. 2002 Dec 6;277(49):47476-85. Epub 2002 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12207020 12207020]
[[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: Vrijbloed, J W.]]
[[Category: Vrijbloed JW]]
[[Category: Zerbe, K.]]
[[Category: Zerbe K]]
[[Category: Zhang, W.]]
[[Category: Zhang W]]
[[Category: oxidative phenol coupling reaction p450 vancomycin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:02:12 2008''

Latest revision as of 16:26, 13 March 2024

Crystal structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin BiosynthesisCrystal structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin Biosynthesis

Structural highlights

1lfk is a 1 chain structure with sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C5B3_AMYOR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1lfk, resolution 1.70Å

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