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• W2024202287 endingPage "1611" @default.
• W2024202287 startingPage "1606" @default.
• W2024202287 abstract "rv1098c, an essential gene in Mycobacterium tuberculosis, codes for a class II fumarase. We describe here the crystal structure of Rv1098c in complex with l-malate, fumarate or the competitive inhibitor meso-tartrate. The models reveal that substrate binding promotes the closure of the active site through conformational changes involving the catalytic SS-loop and the C-terminal domain, which likely represents a general feature of this enzyme superfamily. Analysis of ligand-enzyme interactions as well as site-directed mutagenesis suggest Ser318 as one of the two acid-base catalysts." @default.
• W2024202287 created "2016-06-24" @default.
• W2024202287 creator A5011893335 @default.
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• W2024202287 creator A5075457982 @default.
• W2024202287 creator A5084388900 @default.
• W2024202287 date "2012-05-03" @default.
• W2024202287 modified "2023-10-16" @default.
• W2024202287 title "Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from<i>Mycobacterium tuberculosis</i>" @default.
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• W2024202287 doi "https://doi.org/10.1016/j.febslet.2012.04.034" @default.
• W2024202287 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22561013" @default.
• W2024202287 hasPublicationYear "2012" @default.
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