7qan

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'''Unreleased structure'''
 
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The entry 7qan is ON HOLD until Paper Publication
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==Cytochrome P450 Enzyme AbyV==
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<StructureSection load='7qan' size='340' side='right'caption='[[7qan]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7qan]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_maris_AB-18-032 Micromonospora maris AB-18-032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QAN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qan OCA], [https://pdbe.org/7qan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qan RCSB], [https://www.ebi.ac.uk/pdbsum/7qan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qan ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F4F6Q5_MICM1 F4F6Q5_MICM1]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Abyssomicin C and its atropisomer are potent inhibitors of bacterial folate metabolism. They possess complex polycyclic structures, and their biosynthesis has been shown to involve several unusual enzymatic transformations. Using a combination of synthesis and in vitro assays we reveal that AbyV, a cytochrome P450 enzyme from the aby gene cluster, catalyses a key late-stage epoxidation required for the installation of the characteristic ether-bridged-core of abyssomicin C. The X-ray crystal structure of AbyV has been determined, which in combination with molecular dynamics simulations provides a structural framework for our functional data. This work demonstrates the power of combining selective carbon-13 labelling with NMR spectroscopy as a sensitive tool to interrogate enzyme-catalysed reactions in vitro with no need for purification.
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Authors:
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The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis.,Devine AJ, Parnell AE, Back CR, Lees NR, Johns ST, Zulkepli AZ, Barringer R, Zorn K, Stach JEM, Crump MP, Hayes MA, van der Kamp MW, Race PR, Willis C Angew Chem Int Ed Engl. 2022 Oct 31. doi: 10.1002/anie.202213053. PMID:36314667<ref>PMID:36314667</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7qan" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Micromonospora maris AB-18-032]]
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[[Category: Back CR]]
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[[Category: Parnell AE]]
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[[Category: Race PR]]

Revision as of 10:36, 30 November 2022

Cytochrome P450 Enzyme AbyV

PDB ID 7qan

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