Vancomycin forms ligand-mediated supramolecular complexes.

ABSTRACT: The emergence of resistance to vancomycin and related glycopeptide antibiotics is spurring efforts to develop new antimicrobial therapeutics. High-resolution structural information about antibiotic-ligand recognition should prove valuable in the rational design of improved drugs. We have determined the X-ray crystal structure of the complex of vancomycin with N-acetyl-D-Ala-D-Ala, a mimic of the natural muramyl peptide target, and refined this structure at a resolution of 1.3 A to R and R(free) values of 0.172 and 0.195, respectively. The crystal asymmetric unit contains three back-back vancomycin dimers; two of these dimers participate in ligand-mediated face-face interactions that produce an infinite chain of molecules running throughout the crystal. The third dimer packs against the sid

SUBMITTER: Loll PJ 

PROVIDER: S-EPMC2650734 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature