Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.

ABSTRACT: Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-A resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orient

SUBMITTER: Sung MT 

PROVIDER: S-EPMC2689995 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature