4tvf
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4tvf is ON HOLD Authors: Haslinger, K, Cryle, Max J. Description: OxyB from Actinoplanes teichomyceticus) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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 with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_teichomyceticus Actinoplanes teichomyceticus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4TVF 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]] 1.9Å</td></tr> | ||
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvf OCA], [https://pdbe.org/4tvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tvf RCSB], [https://www.ebi.ac.uk/pdbsum/4tvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tvf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q70AY8_ACTTI Q70AY8_ACTTI] | ||
| + | <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> | ||
| + | <div class="pdbe-citations 4tvf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinoplanes teichomyceticus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cryle MJ]] | ||
| + | [[Category: Haslinger K]] | ||
Current revision
OxyB from Actinoplanes teichomyceticus
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