2MHK

E. coli LpoA N-terminal domain

Summary for 2MHK

• Entry DOI: 10.2210/pdb2mhk/pdb
• Related: 3CKM
• NMR Information: BMRB: 18853
• Descriptor: Penicillin-binding protein activator LpoA (1 entity in total)
• Functional Keywords: lpoa, tpr-like fold, protein binding
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Lipid-anchor; Periplasmic side: P45464
• Total number of polymer chains: 1
• Total formula weight: 28046.50

Authors

Jean, N.L.,Bougault, C.,Lodge, A.,Derouaux, A.,Callens, G.,Egan, A.,Lewis, R.J.,Vollmer, W.,Simorre, J. (deposition date: 2013-11-26, release date: 2014-06-25, Last modification date: 2024-05-15)

Primary citation

Jean, N.L.,Bougault, C.M.,Lodge, A.,Derouaux, A.,Callens, G.,Egan, A.J.,Ayala, I.,Lewis, R.J.,Vollmer, W.,Simorre, J.P.
Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation.
Structure, 22:1047-1054, 2014

PubMed Abstract: 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.

PubMed: 24954617
DOI: 10.1016/j.str.2014.04.017

Experimental method

SOLUTION NMR