Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation

[en] The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-α-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat (TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Jean, Nicolas

Bougault, Catherine

Lodge, Adam

Derouaux, Adeline ; Université de Liège - ULiège > GIGA-R : Virologie - Immunologie

Callens, Gilles

Egan, Alexander

Ayala, Isabel

Lewis, Richard

Vollmer, Waldemar

Simorre, Jean-Pierre

Language :

English

Title :

Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation

Publication date :

July 2014

Journal title :

Structure

ISSN :

0969-2126

eISSN :

1878-4186

Publisher :

Cell Press, Cambridge, United States - Massachusetts

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 05 January 2015

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