Structural highlights
Publication Abstract from PubMed
Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 A 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 alpha-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.
X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis.,VanDuinen AJ, Winchell KR, Keithly ME, Cook PD Biochemistry. 2014 Dec 18. PMID:25496067[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ VanDuinen AJ, Winchell KR, Keithly ME, Cook PD. X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis. Biochemistry. 2014 Dec 18. PMID:25496067 doi:http://dx.doi.org/10.1021/bi501394q
