3VMA: Crystal Structure Of The Full-Length Transglycosylase Pbp1b From Escherichia Coli

Citation:
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.
PDB ID: 3VMADownload
MMDB ID: 98018
PDB Deposition Date: 2011/12/9
Updated in MMDB: 2012/03
Experimental Method:
x-ray diffraction
Resolution: 2.16  Å
Source Organism:
Similar Structures:
Biological Unit for 3VMA: monomeric; determined by author and by software (PISA)
Molecular Components in 3VMA
Label Count Molecule
Protein (1 molecule)
1
Penicillin-binding Protein 1B(Gene symbol: mrcB)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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