X-ray crystallographic structure of BshB, the zinc-dependent deacetylase involved in bacillithiol biosynthesis

Autor:	Robert L. Woodward, Michaela M. Castleman, Chelsea E. Meloche, Mary E. Karpen, Clare G. Carlson, William H. Yobi, Jacqueline C. Jepsen, Benjamin W. Lewis, Brooke N. Zarnosky, Paul D. Cook
Rok vydání:	2019
Předmět:	Models Molecular Glucosamine Zinc Bacterial Proteins Protein Conformation Biocatalysis Cysteine Crystallography X-Ray Protein Structure Reports Molecular Biology Biochemistry Amidohydrolases Bacillus subtilis
Zdroj:	Protein Sci
ISSN:	1469-896X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6564b8e32102c68ad7c544b546ce14 https://pubmed.ncbi.nlm.nih.gov/31867856 Zobrazit plný text záznamu Plný text