title: X-ray crystallographic structure of BshC, a unique enzyme involved in bacillithiol biosynthesis.
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.
authors.affiliation: Department of Cell & Molecular Biology, Grand Valley State University , Allendale, Michigan 49401, United States.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: VanDuinen
authors.forename: Kelsey R
authors.initials: KR
authors.lastname: Winchell
authors.forename: Mary E
authors.initials: ME
authors.lastname: Keithly
authors.forename: Paul D
authors.initials: PD
authors.lastname: Cook
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000378:metabolism; D001412:Bacillus subtilis / Q000737:chemistry* / Q000201:enzymology* / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D005944:Glucosamine / Q000031:analogs & derivatives* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D055503:Protein Multimerization
chemical_list: C543521:bacillithiol; D000604:Amino Acyl-tRNA Synthetases; C019975:cysteinyl-tRNA synthetase; D003545:Cysteine; D005944:Glucosamine