7sfn
From Proteopedia
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<StructureSection load='7sfn' size='340' side='right'caption='[[7sfn]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='7sfn' size='340' side='right'caption='[[7sfn]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[7sfn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SFN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7sfn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avermitilis Streptomyces avermitilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SFN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> | + | </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=MLT:D-MALATE'>MLT</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=7sfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sfn OCA], [https://pdbe.org/7sfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sfn RCSB], [https://www.ebi.ac.uk/pdbsum/7sfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sfn ProSAT]</span></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=7sfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sfn OCA], [https://pdbe.org/7sfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sfn RCSB], [https://www.ebi.ac.uk/pdbsum/7sfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sfn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q93HI7_STRAX Q93HI7_STRAX] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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> | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Streptomyces avermitilis]] |
| - | [[Category: | + | [[Category: Bilyk O]] |
| - | [[Category: | + | [[Category: Dias MVB]] |
| - | [[Category: | + | [[Category: Leadlay PF]] |
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Current revision
Crystal structure of OlmO, a spirocyclase involved in the biosynthesis of oligomycin
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