6ull | pdb_00006ull

BshB from Bacillus subtilis complexed with a substrate analogue

spinqualitylabelsall models 6ull, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ull 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 1.45Å Ligands: RWI, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BSHB1_BACSU Involved in bacillithiol (BSH) biosynthesis. Catalyzes the second step of the pathway, the deacetylation of N-acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal).[UniProtKB:Q81ST8] Publication Abstract from PubMed Many gram-positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three-enzyme pathway that includes the action of the zinc-dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X-ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism. X-ray crystallographic structure of BshB, the zinc-dependent deacetylase involved in bacillithiol biosynthesis.,Woodward RL, Castleman MM, Meloche CE, Karpen ME, Carlson CG, Yobi WH, Jepsen JC, Lewis BW, Zarnosky BN, Cook PD Protein Sci. 2019 Dec 22. doi: 10.1002/pro.3808. PMID:31867856 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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