3FWL

Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli

Summary for 3FWL

• Entry DOI: 10.2210/pdb3fwl/pdb
• Related: 3FWM
• Descriptor: Penicillin-binding protein 1B, MOENOMYCIN (2 entities in total)
• Functional Keywords: bacterial cell wall synthesis, penicillin-binding protein, antibiotics design, alternative initiation, antibiotic resistance, cell inner membrane, cell membrane, cell shape, cell wall biogenesis/degradation, glycosyltransferase, hydrolase, membrane, multifunctional enzyme, peptidoglycan synthesis, signal-anchor, transferase, transmembrane
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Single-pass type II membrane protein: P02919
• Total number of polymer chains: 1
• Total formula weight: 86446.79

Authors

Sung, M.T.,Lai, Y.T.,Huang, C.Y.,Chou, L.Y.,Wong, C.H.,Ma, C. (deposition date: 2009-01-19, release date: 2009-06-02, Last modification date: 2024-10-30)

Primary citation

Sung, M.T.,Lai, Y.T.,Huang, C.Y.,Chou, L.Y.,Shih, H.W.,Cheng, W.C.,Wong, C.H.,Ma, C.
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.
Proc.Natl.Acad.Sci.USA, 106:8824-8829, 2009

PubMed 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.

PubMed: 19458048
DOI: 10.1073/pnas.0904030106

Experimental method

X-RAY DIFFRACTION (3.086 Å)