4tvf
From Proteopedia
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| - | ''' | + | ==OxyB from Actinoplanes teichomyceticus== |
| + | <StructureSection load='4tvf' size='340' side='right' caption='[[4tvf]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tvf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TVF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tvf RCSB], [http://www.ebi.ac.uk/pdbsum/4tvf PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial cytochrome P450s form a remarkable clade of the P450 superfamily of oxidative hemoproteins, and are often involved in the biosynthesis of complex natural products. Those in a subgroup known as "Oxy enzymes" play a crucial role in the biosynthesis of glycopeptide antibiotics, including vancomycin and teicoplanin. The Oxy enzymes catalyze crosslinking of aromatic residues in the non-ribosomal antibiotic precursor peptide while it remains bound to the non-ribosomal peptide synthetase (NRPS); this crosslinking secures the three-dimensional structure of the glycopeptide, crucial for antibiotic activity. We have characterized OxyBtei , the first of the Oxy enzymes in teicoplanin biosynthesis. Our results reveal that OxyBtei possesses a structure similar to those of other Oxy proteins and is active in crosslinking NRPS-bound peptide substrates. However, OxyBtei displays a significantly altered activity spectrum against peptide substrates compared to its well-studied vancomycin homologue. | ||
| - | + | Cytochrome P450 OxyB Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis.,Haslinger K, Maximowitsch E, Brieke C, Koch A, Cryle MJ Chembiochem. 2014 Oct 30. doi: 10.1002/cbic.201402441. PMID:25358800<ref>PMID:25358800</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Unspecific monooxygenase]] | ||
| + | [[Category: Cryle, M J]] | ||
| + | [[Category: Haslinger, K]] | ||
| + | [[Category: Cytochrome p450 phenolic coupling enzyme teicoplanin biosynthesis]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:00, 12 November 2014
OxyB from Actinoplanes teichomyceticus
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