Structure and function of the genomically encoded fosfomycin resistance enzyme, FosB, from Staphylococcus aureus.
作者： Matthew K. Thompson , Mary E. Keithly , Michael C. Goodman , Neal D. Hammer , Paul D. Cook
DOI: 10.1021/BI4015852
关键词:
摘要: The Gram-positive pathogen Staphylococcus aureus is a leading cause of global morbidity and mortality. Like many multi-drug-resistant organisms, S. contains antibiotic-modifying enzymes that facilitate resistance to multitude antimicrobial compounds. FosB Mn2+-dependent fosfomycin-inactivating enzyme found in catalyzes nucleophilic addition either l-cysteine (l-Cys) or bacillithiol (BSH) the antibiotic, resulting modified compound with no bactericidal properties. three-dimensional X-ray crystal structure from (FosBSa) has been determined resolution 1.15 A. Cocrystallization FosBSa l-Cys BSH results disulfide bond between exogenous thiol active site Cys9 enzyme. An analysis structures suggests highly conserved loop region must change conformation bind fosfomycin. While two crystals contain Zn2+ site, kinetic analyses indica...
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