X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis | Zendy

Andrew J. VanDuinen | Zendy; Kelsey R. Winchell | Zendy; M.E. Keithly | Zendy; P.D. Cook | Zendy

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X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis

Author(s) -

Andrew J. VanDuinen,

Kelsey R. Winchell,

M.E. Keithly,

P.D. Cook

Publication year - 2014

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi501394q

Subject(s) - enzyme , dna ligase , chemistry , biosynthesis , coiled coil , stereochemistry , cysteine , crystal structure , oxidoreductase , protein structure , peptide , active site , biochemistry , crystallography

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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