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2OQO

Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis

Summary for 2OQO
Entry DOI10.2210/pdb2oqo/pdb
DescriptorPenicillin-binding protein 1A (PBP-1a) (PBP1a), 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ... (4 entities in total)
Functional Keywordstransferase
Biological sourceAquifex aeolicus
Cellular locationCell inner membrane ; Single- pass type II membrane protein : O66874
Total number of polymer chains1
Total formula weight23765.61
Authors
Yuan, Y.,Sliz, P.,Walker, S. (deposition date: 2007-01-31, release date: 2007-03-13, Last modification date: 2023-12-27)
Primary citationYuan, 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: 17360321
DOI: 10.1073/pnas.0701160104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

226707

數據於2024-10-30公開中

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