Document Detail

Vancomycin: Ligand recognition, Dimerization and Super-complex Formation.
MedLine Citation:
PMID:  23298227     Owner:  NLM     Status:  Publisher    
The antibiotic vancomycin targets lipid II blocking cell wall synthesis in Gram-positive bacteria. Despite extensive study, questions remain regarding how it recognizes its primary ligand and what is the most biologically relevant form of vancomycin. In this work molecular dynamics simulation techniques have been used to examine the process of ligand binding and dimerization of vancomycin. Starting from one or more vancomycin monomers in solution together with different peptide ligands derived from lipid II the simulations predict the structures of the ligated monomeric and dimeric complexes to within 0.1 nm root-mean-squared deviation of the structures determined experimentally. The simulations reproduce the conformation transitions observed by NMR and suggest that proposed differences between the crystal structure and the solution structure are an artifact of the way the NMR data has been interpreted in terms of a structural model. The spontaneous formation of both back-to-back and face-to-face dimers was observed in the simulation. This has allowed a detailed analysis of the origin of the cooperatively between ligand binding and dimerization and suggest that the formation of face-to-face dimers could be functionally significant. The work also highlights the possible role of structural water in stabilizing the vancomycin ligand complexes and their role in the manifestation of vancomycin resistance. © 2013 The Authors Journal compilation © 2013 FEBS.
Zhiguang Jia; Megan O'Mara; Johannes Zuegg; Matthew A Cooper; Alan E Mark
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-9
Journal Detail:
Title:  The FEBS journal     Volume:  -     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-9     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2013 The Authors Journal compilation © 2013 FEBS.
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.
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