1S62

Solution structure of the Escherichia coli TolA C-terminal domain

1S62 の概要

• エントリーDOI: 10.2210/pdb1s62/pdb
• NMR情報: BMRB: 4771
• 分子名称: TolA protein (1 entity in total)
• 機能のキーワード: tol g3p interaction, protein transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Single-pass type II membrane protein: P19934
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11329.83

構造登録者

Deprez, C.,Blanchard, L.,Simorre, J.-P.,Gavioli, M.,Guerlesquin, F.,Lazdunski, C.,Lloubes, R.,Marion, D. (登録日: 2004-01-22, 公開日: 2005-02-15, 最終更新日: 2024-11-20)

主引用文献

Deprez, C.,Lloubes, R.,Gavioli, M.,Marion, D.,Guerlesquin, F.,Blanchard, L.
Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain.
J.Mol.Biol., 346:1047-1057, 2005

PubMed Abstract: The Tol-Pal system of Escherichia coli is a macromolecular complex located in the cell envelope. It is involved in maintaining the integrity of the outer membrane and is required for the uptake of two different types of macromolecules, which are bacteriotoxins (colicins) and DNA of filamentous bacteriophages. The TolA protein plays a central role in these import mechanisms. Its C-terminal domain (TolAIII) is involved in the translocation step via direct interaction with the N-terminal domain of colicins and the N-terminal domain of the phage minor coat gene 3 protein (g3pN1). Extreme behaviours of TolAIII have been previously observed, since the structure of TolAIII either remained unaffected or adopted disordered conformation upon binding to different pore-forming colicins. Here, we have solved the 3D structure of free TolAIII by heteronuclear NMR spectroscopy and compared it to the crystal structure of TolAIII bound to g3pN1 in order to study the effect of g3pN1 on the tertiary structure of TolAIII. Backbone 1H, 15N and 13C resonances of the g3pN1-bound TolAIII were also assigned and used to superimpose the solution structure of free TolAIII on the crystal structure of the g3pN1-TolAIII fusion protein. This allowed us to track conformational changes of TolAIII upon binding. While the global fold of free TolAIII is mainly identical to that of g3pN1-bound TolAIII, shift of secondary structures does occur. Thus, TolAIII, which interacts also in vivo with Pal and TolB, is able to adapt its conformation upon binding to various partners. Possible models for protein binding mechanisms are discussed to explain this so-far unobserved behaviour of TolAIII.

PubMed: 15701516
DOI: 10.1016/j.jmb.2004.12.028

実験手法

SOLUTION NMR