Summary for 3VMA
| Entry DOI | 10.2210/pdb3vma/pdb |
| Related | 3FWL |
| Descriptor | Penicillin-binding protein 1B, MOENOMYCIN (3 entities in total) |
| Functional Keywords | bacterial cell wall synthesis, penicillin-binding protein, antibiotics design, pbp3, mipa, mlta, ftsn, membrane, transferase, hydrolase-antibiotic complex, hydrolase/antibiotic |
| 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 | 87163.48 |
| Authors | Huang, C.Y.,Sung, M.T.,Lai, Y.T.,Chou, L.Y.,Shih, H.W.,Cheng, W.C.,Wong, C.H.,Ma, C. (deposition date: 2011-12-09, release date: 2012-03-14, Last modification date: 2023-11-08) |
| 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 Cited by 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: 19458048DOI: 10.1073/pnas.0904030106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.161 Å) |
Structure validation
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