title: Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
abstract: Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to maintain osmotic stability and cell shape. PG is assembled from lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed by PG synthases, which are anchored to the cytoplasmic membrane and are controlled from inside the cell by cytoskeletal elements. Recently, two lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for activating the main peptidoglycan synthases, Penicillin-Binding Proteins 1A and 1B, from the outer membrane. Here we present the backbone and side-chain assignment of the (1)H, (13)C and (15)N resonances of LpoB from E. coli. We also provide evidence for a two-domain organization of LpoB and a largely disordered, 64 amino acid-long N-terminal domain.
authors.affiliation: Institut de Biologie Structurale Jean-Pierre Ebel, Université Grenoble Alpes, EPN Campus, 6 rue Jules Horowitz, 38027, Grenoble, France.
authors.forename: Nicolas L
authors.initials: NL
authors.lastname: Jean
authors.forename: Catherine M
authors.initials: CM
authors.lastname: Bougault
authors.forename: Alexander J F
authors.initials: AJ
authors.lastname: Egan
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Simorre
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004926:Escherichia coli / Q000166:cytology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012996:Solutions
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C000592364:LpoB protein, E coli; D012996:Solutions