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

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

    Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C.

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

    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 [PubMed - indexed for MEDLINE]

    PMCID: 2689995

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