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

Abstract

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.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
980098
Report Number(s):
BNL-93016-2010-JA
TRN: US201015%%1483
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Proteins: Structure, Functions, and Bioinformatics
Additional Journal Information:
Journal Volume: 72; Journal Issue: 3
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BACTERIA; CELL WALL; CRYSTAL STRUCTURE; ENZYMES; POLYMERS; POTENTIALS; RABBITS; RATS; TARGETS; national synchrotron light source

Citation Formats

Ragumani, S, Kumaran, D, Burley, S, and Swaminathan, S. Crystal Structure of a Putative Lysostaphin Peptidase from Vibrio cholerae. United States: N. p., 2008. Web. doi:10.1002/prot.22095.
Ragumani, S, Kumaran, D, Burley, S, & Swaminathan, S. Crystal Structure of a Putative Lysostaphin Peptidase from Vibrio cholerae. United States. https://doi.org/10.1002/prot.22095
Ragumani, S, Kumaran, D, Burley, S, and Swaminathan, S. 2008. "Crystal Structure of a Putative Lysostaphin Peptidase from Vibrio cholerae". United States. https://doi.org/10.1002/prot.22095.
@article{osti_980098,
title = {Crystal Structure of a Putative Lysostaphin Peptidase from Vibrio cholerae},
author = {Ragumani, S and Kumaran, D and Burley, S and Swaminathan, S},
abstractNote = {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.},
doi = {10.1002/prot.22095},
url = {https://www.osti.gov/biblio/980098}, journal = {Proteins: Structure, Functions, and Bioinformatics},
number = 3,
volume = 72,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 2008},
month = {Tue Jan 01 00:00:00 EST 2008}
}