7ei3

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m (Protected "7ei3" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 7ei3 is ON HOLD
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==Crystal structure of MasL, a thiolase from Massilia sp. YMA4==
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<StructureSection load='7ei3' size='340' side='right'caption='[[7ei3]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7ei3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Empedobacter_haloabium Empedobacter haloabium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EI3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</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=7ei3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ei3 OCA], [https://pdbe.org/7ei3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ei3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ei3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ei3 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial polyynes are highly active natural products with a broad spectrum of antimicrobial activities. However, their detailed mechanism of action remains unclear. By integrating comparative genomics, transcriptomics, functional genetics, and metabolomics analysis, we identified a unique polyyne resistance gene, masL (encoding acetyl-CoA acetyltransferase), in the biosynthesis gene cluster of antifungal polyynes (massilin A 1, massilin B 2, collimonin C 3, and collimonin D 4) of Massilia sp. YMA4. Crystallographic analysis indicated that bacterial polyynes serve as covalent inhibitors of acetyl-CoA acetyltransferase. Moreover, we confirmed that the bacterial polyynes disrupted cell membrane integrity and inhibited the cell viability of Candida albicans by targeting ERG10, the homolog of MasL. Thus, this study demonstrated that acetyl-CoA acetyltransferase is a potential target for developing antifungal agents.
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Authors:
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Integrated omics approach to unveil antifungal bacterial polyynes as acetyl-CoA acetyltransferase inhibitors.,Lin CC, Hoo SY, Ma LT, Lin C, Huang KF, Ho YN, Sun CH, Lee HJ, Chen PY, Shu LJ, Wang BW, Hsu WC, Ko TP, Yang YL Commun Biol. 2022 May 12;5(1):454. doi: 10.1038/s42003-022-03409-6. PMID:35551233<ref>PMID:35551233</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 7ei3" 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: Huang KF]]
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[[Category: Lin CC]]
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[[Category: Yang YL]]

Current revision

Crystal structure of MasL, a thiolase from Massilia sp. YMA4

PDB ID 7ei3

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