7xrq

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'''Unreleased structure'''
 
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The entry 7xrq is ON HOLD until Paper Publication
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==The Catalytic Core Structure of Cystathionine beta-Synthase from Candida albicans==
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<StructureSection load='7xrq' size='340' side='right'caption='[[7xrq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7xrq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XRQ 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=PO4:PHOSPHATE+ION'>PO4</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=7xrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xrq OCA], [https://pdbe.org/7xrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xrq RCSB], [https://www.ebi.ac.uk/pdbsum/7xrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xrq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q59T95_CANAL Q59T95_CANAL]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The global emergence of antifungal resistance threatens the limited arsenal of available treatments and emphasizes the urgent need for alternative antifungal agents. Targeting fungal pathogenic functions is an appealing alternative therapeutic strategy. Here, we show that cystathionine beta-synthase (CBS), compared with cystathionine gamma-lyase, is the major enzyme that synthesizes hydrogen sulfide in the pathogenic fungus Candida albicans. Deletion of CBS leads to deficiencies in resistance to oxidative stress, retarded cell growth, defective hyphal growth, and increased beta-glucan exposure, which, together, reduce the pathogenicity of C. albicans. By high-throughput screening, we identified protolichesterinic acid, a natural molecule obtained from a lichen, as an inhibitor of CBS that neutralizes the virulence of C. albicans and exhibits therapeutic efficacy in a murine candidiasis model. These findings support the application of CBS as a potential therapeutic target to fight fungal infections.
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Authors: Lou, H.X., Yu, H.N., Chang, W.Q.
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Inhibition of fungal pathogenicity by targeting the H(2)S-synthesizing enzyme cystathionine beta-synthase.,Chang W, Zhang M, Jin X, Zhang H, Zheng H, Zheng S, Qiao Y, Yu H, Sun B, Hou X, Lou H Sci Adv. 2022 Dec 16;8(50):eadd5366. doi: 10.1126/sciadv.add5366. Epub 2022 Dec , 16. PMID:36525499<ref>PMID:36525499</ref>
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Description: The Catalytic Core Structure of Cystathionine beta-Synthase from Candida albicans
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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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[[Category: Lou, H.X]]
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<div class="pdbe-citations 7xrq" style="background-color:#fffaf0;"></div>
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[[Category: Chang, W.Q]]
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== References ==
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[[Category: Yu, H.N]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Candida albicans SC5314]]
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[[Category: Large Structures]]
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[[Category: Chang WQ]]
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[[Category: Lou HX]]
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[[Category: Yu HN]]

Revision as of 09:21, 19 April 2023

The Catalytic Core Structure of Cystathionine beta-Synthase from Candida albicans

PDB ID 7xrq

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