6ULL

BshB from Bacillus subtilis complexed with a substrate analogue

6ULL の概要

• エントリーDOI: 10.2210/pdb6ull/pdb
• 関連するPDBエントリー: 6P2T
• 分子名称: 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)
• 機能のキーワード: bacillithiol, deacetylase, gram-positive, hydrolase, hydroxamic acid
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29202.45

構造登録者

Cook, P.D.,Castleman, M.M.,Woodward, R.L. (登録日: 2019-10-08, 公開日: 2020-01-08, 最終更新日: 2023-10-11)

主引用文献

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

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: 31867856
DOI: 10.1002/pro.3808

実験手法

X-RAY DIFFRACTION (1.45 Å)