2OQO
Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis
Summary for 2OQO
Entry DOI | 10.2210/pdb2oqo/pdb |
Descriptor | Penicillin-binding protein 1A (PBP-1a) (PBP1a), 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ... (4 entities in total) |
Functional Keywords | transferase |
Biological source | Aquifex aeolicus |
Cellular location | Cell inner membrane ; Single- pass type II membrane protein : O66874 |
Total number of polymer chains | 1 |
Total formula weight | 23765.61 |
Authors | Yuan, Y.,Sliz, P.,Walker, S. (deposition date: 2007-01-31, release date: 2007-03-13, Last modification date: 2023-12-27) |
Primary citation | Yuan, Y.,Barrett, D.,Zhang, Y.,Kahne, D.,Sliz, P.,Walker, S. Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc.Natl.Acad.Sci.Usa, 104:5348-5353, 2007 Cited by PubMed Abstract: Peptidoglycan is an essential polymer that forms a protective shell around bacterial cell membranes. Peptidoglycan biosynthesis is the target of many clinically used antibiotics, including the beta-lactams, imipenems, cephalosporins, and glycopeptides. Resistance to these and other antibiotics has prompted interest in an atomic-level understanding of the enzymes that make peptidoglycan. Representative structures have been reported for most of the enzymes in the pathway. Until now, however, there have been no structures of any peptidoglycan glycosyltransferases (also known as transglycosylases), which catalyze formation of the carbohydrate chains of peptidoglycan from disaccharide subunits on the bacterial cell surface. We report here the 2.1-A crystal structure of the peptidoglycan glycosyltransferase (PGT) domain of Aquifex aeolicus PBP1A. The structure has a different fold from all other glycosyltransferase structures reported to date, but it bears some resemblance to lambda-lysozyme, an enzyme that degrades the carbohydrate chains of peptidoglycan. An analysis of the structure, combined with biochemical information showing that these enzymes are processive, suggests a model for glycan chain polymerization. PubMed: 17360321DOI: 10.1073/pnas.0701160104 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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