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Title: Crystal Structure of a Putative Lysostaphin Peptidase from Vibrio cholerae

Journal Article · · Proteins: Structure, Functions, and Bioinformatics
DOI:https://doi.org/10.1002/prot.22095· OSTI ID:980098

Peptidoglycan (PGN) constitutes the cell walls of virtually all bacteria, making it a target of the innate immune system. PGN is a polymer of alternating {Beta} (1{yields}4) linked N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc), crossbridged by oligopeptide stems. Lysotaphin type enzymes are believed to cleave the glycl-glycine and glycyl-alanine bonds that occur in glycine-rich cross-bridges. Lysostaphins represent potential anti staphylococcal agents. Specifically, they can eradicate S.aureus nasal colonization in the rat model and are effective in treating methicillin-resistant S. aureus endophthalmitis in rabbits. These enzymes belong to the metalloendopeptidase family and possess a conserved HXH active site motif.

Research Organization:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Organization:
Doe - Office Of Science
DOE Contract Number:
DE-AC02-98CH10886
OSTI ID:
980098
Report Number(s):
BNL-93016-2010-JA; TRN: US201015%%1483
Journal Information:
Proteins: Structure, Functions, and Bioinformatics, Vol. 72, Issue 3
Country of Publication:
United States
Language:
English