Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: implications for PBP1A stimulation. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Structure Année : 2014

Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: implications for PBP1A stimulation.

Résumé

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.
Fichier non déposé

Dates et versions

hal-01097207 , version 1 (19-12-2014)

Identifiants

  • HAL Id : hal-01097207 , version 1
  • PUBMED : 24954617

Citer

Nicolas L Jean, Catherine M Bougault, Adam Lodge, Adeline Derouaux, Gilles Callens, et al.. Elongated structure of the outer-membrane activator of peptidoglycan synthesis LpoA: implications for PBP1A stimulation.. Structure, 2014, pp.1047-54. ⟨hal-01097207⟩
69 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More