2OLU
Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme
Summary for 2OLU
| Entry DOI | 10.2210/pdb2olu/pdb |
| Related | 2OLV |
| Descriptor | Penicillin-binding protein 2, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | transpeptidase fold glycosyltransferase family 51, lysozyme fold, transferase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 74702.21 |
| Authors | Lovering, A.L.,De Castro, L.H.,Lim, D.,Strynadka, N.C. (deposition date: 2007-01-19, release date: 2007-03-20, Last modification date: 2024-11-20) |
| Primary citation | Lovering, A.L.,de Castro, L.H.,Lim, D.,Strynadka, N.C. Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science, 315:1402-1405, 2007 Cited by PubMed Abstract: Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition. PubMed: 17347437DOI: 10.1126/science.1136611 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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