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X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis
Author(s) -
Woodward Robert L.,
Castleman Michaela M.,
Meloche Chelsea E.,
Karpen Mary E.,
Carlson Clare G.,
Yobi William H.,
Jepsen Jacqueline C.,
Lewis Benjamin W.,
Zarnosky Brooke N.,
Cook Paul D.
Publication year - 2020
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3808
Subject(s) - bacillus subtilis , fosfomycin , histidine , enzyme , biosynthesis , chemistry , zinc , stereochemistry , active site , biochemistry , binding site , metalloprotein , bacteria , catalysis , biology , antibiotics , organic chemistry , genetics
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.