4wbd | pdb_00004wbd

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

spinqualitylabelsall models 4wbd, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wbd is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.77Å Ligands: ADP, CIT, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BSHC_BACSU Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH.[HAMAP-Rule:MF_01867] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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