title: Regulation of Bacterial Peptidoglycan Polymerization.
abstract: How bacterial cells control the activity of peptidoglycan polymerases has remained mysterious. Biochemical characterization of derivatives of penicillin-binding protein PBP1b that are functional in the absence of lipoprotein LpoB provides evidence for allosteric control of PBP1b glycosyltransferase activity via binding of LpoB to the PBP1b UBH1 domain.
authors.affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR_S 1138, Centre de Recherche des Cordeliers, Equipe 12, F-75006, Paris, France; INSERM, UMR_S 1138, Centre de Recherche des Cordeliers, F-75006, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR_S 1138, Centre de Recherche des Cordeliers, F-75006, Paris, France. Electronic address: michel.arthur@crc.jussieu.fr.
authors.forename: Michel
authors.initials: M
authors.lastname: Arthur
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D046915:Penicillin-Binding Proteins / Q000378:metabolism*; D010457:Peptidoglycan / Q000096:biosynthesis*; D046928:Peptidoglycan Glycosyltransferase / Q000378:metabolism*; D058105:Polymerization; D011485:Protein Binding; D000072417:Protein Domains; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C000592364:LpoB protein, E coli; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan; D046928:Peptidoglycan Glycosyltransferase; C478681:penicillin-binding protein 1B, E coli; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase
keywords: LpoB; PBP1b; glycosyltransferase; lipoprotein; peptidoglycan; transpeptidase