5cxo: Difference between revisions
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<StructureSection load='5cxo' size='340' side='right'caption='[[5cxo]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5cxo' size='340' side='right'caption='[[5cxo]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cxo]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5cxo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CXO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=5cxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cxo OCA], [https://pdbe.org/5cxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cxo RCSB], [https://www.ebi.ac.uk/pdbsum/5cxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cxo ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H6D578_STRA4 H6D578_STRA4] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dias | [[Category: Streptomyces albus]] | ||
[[Category: Hong | [[Category: Dias MVB]] | ||
[[Category: Leadlay | [[Category: Hong H]] | ||
[[Category: Luhavaya | [[Category: Leadlay PF]] | ||
[[Category: Oliveira | [[Category: Luhavaya H]] | ||
[[Category: Williams | [[Category: Oliveira LG]] | ||
[[Category: Williams SR]] | |||
Revision as of 13:12, 21 June 2023
Intriguing role of epoxide hydrolase/cyclase-like enzyme SalBIII in pyran ring formation in polyether salinomycinIntriguing role of epoxide hydrolase/cyclase-like enzyme SalBIII in pyran ring formation in polyether salinomycin
Structural highlights
FunctionPublication Abstract from PubMedTetrahydropyran rings are a common feature of complex polyketide natural products, but much remains to be learned about the enzymology of their formation. The enzyme SalBIII from the salinomycin biosynthetic pathway resembles other polyether epoxide hydrolases/cyclases of the MonB family, but SalBIII plays no role in the conventional cascade of ring opening/closing. Mutation in the salBIII gene gave a metabolite in which ring A is not formed. Using this metabolite in vitro as a substrate analogue, SalBIII has been shown to form pyran ring A. We have determined the X-ray crystal structure of SalBIII, and structure-guided mutagenesis of putative active-site residues has identified Asp38 and Asp104 as an essential catalytic dyad. The demonstrated pyran synthase activity of SalBIII further extends the impressive catalytic versatility of alpha+beta barrel fold proteins. Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis.,Luhavaya H, Dias MV, Williams SR, Hong H, de Oliveira LG, Leadlay PF Angew Chem Int Ed Engl. 2015 Sep 17. doi: 10.1002/anie.201507090. PMID:26377145[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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