X-ray crystallographic structure of BshC, a unique enzyme involved in bacillithiol biosynthesis.
Biochemistry. 2015 Jan 20;54(2):100-3. doi:10.1021/bi501394q. Epub 2014 Dec 18
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摘要
Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 à resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core Rossmann fold with connecting peptide motifs (CP1 and CP2) and a unique α-helical coiled-coil domain that facilitates dimerization. The model contains citrate and glycerol in the canonical active site and ADP in a second binding pocket. The overall structure and bound ligands give insight into the function of this unique enzyme.
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基因功能
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原始数据
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文献解读
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