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}
}