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Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8824-9. doi: 10.1073/pnas.0904030106. Epub 2009 May 19.

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

Author information

1
Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Taipei 115, Taiwan.

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 orientation.

PMID:
19458048
PMCID:
PMC2689995
DOI:
10.1073/pnas.0904030106
[Indexed for MEDLINE]
Free PMC Article

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