7xrq

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

spinqualitylabelsall models 7xrq, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xrq is a 2 chain structure with sequence from Candida albicans SC5314. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.501Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q59T95_CANAL Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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