ArticleBiochemistry2015
X-ray crystallographic structure of BshC, a unique enzyme involved in bacillithiol biosynthesis.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- The Role of Bacillithiol in Gram-Positive Firmicutes.Antioxidants & redox signaling · 2018Review
- A Structural, Functional, and Computational Analysis of BshA, the First Enzyme in the Bacillithiol Biosynthesis Pathway.Biochemistry · 2016Article
- Redox regulation by reversible protein S-thiolation in bacteria.Frontiers in microbiology · 2015Review
- Bacillithiol: a key protective thiol in Staphylococcus aureus.Expert review of anti-infective therapy · 2015Review
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Authors and funding
4 authors.
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Abstract
Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å 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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