4WBD

The crystal structure of BshC from Bacillus subtilis complexed with citrate and ADP

Summary for 4WBD

• Entry DOI: 10.2210/pdb4wbd/pdb
• Descriptor: BSHC, ADENOSINE-5'-DIPHOSPHATE, CITRIC ACID, ... (5 entities in total)
• Functional Keywords: bacililthiol, ligase, cysteine, rossmann
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 63652.83

Authors

Cook, P.D.,VanDuinen, A.J.,Winchell, K.R. (deposition date: 2014-09-03, release date: 2014-12-31, Last modification date: 2023-12-27)

Primary citation

VanDuinen, A.J.,Winchell, K.R.,Keithly, M.E.,Cook, P.D.
X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis.
Biochemistry, 54:100-103, 2015

PubMed 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.

PubMed: 25496067
DOI: 10.1021/bi501394q

Experimental method

X-RAY DIFFRACTION (1.77 Å)