View source for 7sfp


==Crystal structure of OssO, a spirocyclase involved in the biosynthesis of ossamycin==
<StructureSection load='7sfp' size='340' side='right'caption='[[7sfp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_ossamyceticus Streptomyces ossamyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SFP 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]] 2.2&#8491;</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=7sfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sfp OCA], [https://pdbe.org/7sfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sfp RCSB], [https://www.ebi.ac.uk/pdbsum/7sfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sfp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A481S8L7_9ACTN A0A481S8L7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A key step in the biosynthesis of numerous polyketides is the stereospecific formation of a spiroacetal (spiroketal). We report here that spiroacetal formation in the biosynthesis of the macrocyclic polyketides ossamycin and oligomycin involves catalysis by a novel spiroacetal cyclase. OssO from the ossamycin biosynthetic gene cluster (BGC) is homologous to OlmO, the product of an unannotated gene from the oligomycin BGC. The deletion of olmO abolished oligomycin production and led to the isolation of oligomycin-like metabolites lacking the spiroacetal structure. Purified OlmO catalyzed complete conversion of the major metabolite into oligomycin C. Crystal structures of OssO and OlmO reveal an unusual 10-strand beta-barrel. Three conserved polar residues are clustered together in the beta-barrel cavity, and site-specific mutation of any of these residues either abolished or substantially diminished OlmO activity, supporting a role for general acid/general base catalysis in spiroacetal formation.

Enzyme-Catalyzed Spiroacetal Formation in Polyketide Antibiotic Biosynthesis.,Bilyk O, Oliveira GS, de Angelo RM, Almeida MO, Honorio KM, Leeper FJ, Dias MVB, Leadlay PF J Am Chem Soc. 2022 Aug 17;144(32):14555-14563. doi: 10.1021/jacs.2c03313. Epub, 2022 Aug 3. PMID:35921248<ref>PMID:35921248</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sfp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces ossamyceticus]]
[[Category: Bilyk O]]
[[Category: Dias MVB]]
[[Category: Leadlay PF]]