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.
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Biomolecular NMR Assignments, Springer, 2015, 9 (1), pp.123-7
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Contributeur : Frank Thomas <>
Soumis le : jeudi 26 novembre 2015 - 08:44:09
Dernière modification le : lundi 19 février 2018 - 14:34:03

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Nicolas L Jean, Catherine M Bougault, Alexander J F Egan, Waldemar Vollmer, Jean-Pierre Simorre. Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.. Biomolecular NMR Assignments, Springer, 2015, 9 (1), pp.123-7. 〈hal-01233985〉

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