2MHK

E. coli LpoA N-terminal domain

2MHK の概要

• エントリーDOI: 10.2210/pdb2mhk/pdb
• 関連するPDBエントリー: 3CKM
• NMR情報: BMRB: 18853
• 分子名称: Penicillin-binding protein activator LpoA (1 entity in total)
• 機能のキーワード: lpoa, tpr-like fold, protein binding
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor; Periplasmic side: P45464
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28046.50

構造登録者

Jean, N.L.,Bougault, C.,Lodge, A.,Derouaux, A.,Callens, G.,Egan, A.,Lewis, R.J.,Vollmer, W.,Simorre, J. (登録日: 2013-11-26, 公開日: 2014-06-25, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR