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| | <StructureSection load='4tvf' size='340' side='right'caption='[[4tvf]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4tvf' size='340' side='right'caption='[[4tvf]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tvf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinoplanes_teichomyceticus"_parenti_et_al._1978 "actinoplanes teichomyceticus" parenti et al. 1978]. 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcp20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1867 "Actinoplanes teichomyceticus" Parenti et al. 1978])</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> |
| - | <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://pdbe.org/4tvf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tvf RCSB], [http://www.ebi.ac.uk/pdbsum/4tvf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tvf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q70AY8_ACTTI Q70AY8_ACTTI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinoplanes teichomyceticus parenti et al. 1978]] | + | [[Category: Actinoplanes teichomyceticus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Unspecific monooxygenase]]
| + | [[Category: Cryle MJ]] |
| - | [[Category: Cryle, M J]] | + | [[Category: Haslinger K]] |
| - | [[Category: Haslinger, K]] | + | |
| - | [[Category: Cytochrome p450 phenolic coupling enzyme teicoplanin biosynthesis]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q70AY8_ACTTI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haslinger K, Maximowitsch E, Brieke C, Koch A, Cryle MJ. Cytochrome P450 OxyB Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis. Chembiochem. 2014 Oct 30. doi: 10.1002/cbic.201402441. PMID:25358800 doi:http://dx.doi.org/10.1002/cbic.201402441
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