5hh3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==OxyA from Actinoplanes teichomyceticus== | |
| + | <StructureSection load='5hh3' size='340' side='right'caption='[[5hh3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hh3]] is a 2 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=5HH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HH3 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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=5hh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hh3 OCA], [https://pdbe.org/5hh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hh3 RCSB], [https://www.ebi.ac.uk/pdbsum/5hh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hh3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6ZZI8_ACTTI Q6ZZI8_ACTTI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cyclization of glycopeptide antibiotic precursors occurs in either three or four steps catalyzed by Cytochrome P450 enzymes. Three of these enzymes have been structurally characterized to date with the second enzyme along the pathway, OxyA, escaping structural analysis. We are now able to present the structure of OxyAtei involved in teicoplanin biosynthesis - the same enzyme recently shown to be the first active OxyA homologue. In spite of the hydrophobic character of the teicoplanin precursor, the polar active site of OxyAtei and its affinity for certain azole inhibitors hint at its preference for substrates with polar decorations. This article is protected by copyright. All rights reserved. | ||
| - | + | Structure of OxyA : completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade.,Haslinger K, Cryle MJ FEBS Lett. 2016 Jan 28. doi: 10.1002/1873-3468.12081. PMID:26820384<ref>PMID:26820384</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cryle | + | <div class="pdbe-citations 5hh3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Haslinger | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinoplanes teichomyceticus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cryle MJ]] | ||
| + | [[Category: Haslinger K]] | ||
Current revision
OxyA from Actinoplanes teichomyceticus
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