3mgx: Difference between revisions
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==Crystal Structure of P450 OxyD that is involved in the Biosynthesis of Vancomycin-type Antibiotics== | ==Crystal Structure of P450 OxyD that is involved in the Biosynthesis of Vancomycin-type Antibiotics== | ||
<StructureSection load='3mgx' size='340' side='right' caption='[[3mgx]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3mgx' size='340' side='right'caption='[[3mgx]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mgx]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mgx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_balhimycina Amycolatopsis balhimycina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MGX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3mgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgx OCA], [https://pdbe.org/3mgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mgx RCSB], [https://www.ebi.ac.uk/pdbsum/3mgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgx ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q939Y1_AMYBA Q939Y1_AMYBA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Amycolatopsis balhimycina]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cryle | [[Category: Cryle MJ]] | ||
[[Category: Schlichting | [[Category: Schlichting I]] | ||
Latest revision as of 19:33, 1 November 2023
Crystal Structure of P450 OxyD that is involved in the Biosynthesis of Vancomycin-type AntibioticsCrystal Structure of P450 OxyD that is involved in the Biosynthesis of Vancomycin-type Antibiotics
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe cytochrome P450 OxyD from the balhimycin glycopeptide antibiotic biosynthetic operon of Amycolatopsis mediterranei is involved in the biosynthesis of the modified amino acid beta-R-hydroxytyrosine, an essential precursor for biosynthesis of the vancomycin-type aglycone. OxyD binds the substrate tyrosine not free in solution, but rather covalently linked to the carrier protein (CP) domain of the non-ribosomal peptide synthase BpsD, exhibiting micromolar binding affinity to a tyrosine-loaded carrier protein construct. The crystal structure of OxyD was determined to 2.1-A resolution, revealing a potential binding site for the carrier protein-bound substrate in a different orientation to that seen with the acyl carrier protein-bound P450(BioI) (Cryle, M. J., and Schlichting, I. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 15696-15701). A series of residues were identified across known aminoacyl-CP-oxidizing P450s that are highly conserved and cluster in the active site or potential CP binding site of OxyD. These residues appear to be characteristic for aminoacyl-CP-oxidizing P450s, allowing sequence based identification of P450 function for this subgroup of P450s that play vital roles in the biosyntheses of many important natural products in addition to the vancomycin-type antibiotics. The ability to analyze such P450 function based upon sequence data alone should prove an important tool in the analysis and identification of new medicinally relevant biomolecules. Structural characterization of OxyD, a cytochrome P450 involved in beta-hydroxytyrosine formation in vancomycin biosynthesis.,Cryle MJ, Meinhart A, Schlichting I J Biol Chem. 2010 Aug 6;285(32):24562-74. Epub 2010 Jun 1. PMID:20519494[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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