6ULL
BshB from Bacillus subtilis complexed with a substrate analogue
Summary for 6ULL
| Entry DOI | 10.2210/pdb6ull/pdb |
| Related | 6P2T |
| Descriptor | N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1, (2S)-2-({2-deoxy-2-[(hydroxycarbamoyl)amino]-alpha-D-glucopyranosyl}oxy)butanedioic acid, ZINC ION, ... (5 entities in total) |
| Functional Keywords | bacillithiol, deacetylase, gram-positive, hydrolase, hydroxamic acid |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 1 |
| Total formula weight | 29202.45 |
| Authors | Cook, P.D.,Castleman, M.M.,Woodward, R.L. (deposition date: 2019-10-08, release date: 2020-01-08, Last modification date: 2023-10-11) |
| Primary citation | Woodward, R.L.,Castleman, M.M.,Meloche, C.E.,Karpen, M.E.,Carlson, C.G.,Yobi, W.H.,Jepsen, J.C.,Lewis, B.W.,Zarnosky, B.N.,Cook, P.D. X-ray crystallographic structure of BshB, the zinc-dependent deacetylase involved in bacillithiol biosynthesis. Protein Sci., 29:1035-1039, 2020 Cited by PubMed Abstract: 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. PubMed: 31867856DOI: 10.1002/pro.3808 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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