2LHK

Structural analysis of a chaperone in type III secretion system

2LHK の概要

• エントリーDOI: 10.2210/pdb2lhk/pdb
• NMR情報: BMRB: 17856
• 分子名称: L0052 (1 entity in total)
• 機能のキーワード: helical bundle, chaperone, type iii secretion system
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24640.25

構造登録者

Chen, L.,Economou, A.,Kalodimos, C.G. (登録日: 2011-08-11, 公開日: 2011-12-28, 最終更新日: 2024-05-15)

主引用文献

Chen, L.,Balabanidou, V.,Remeta, D.P.,Minetti, C.A.,Portaliou, A.G.,Economou, A.,Kalodimos, C.G.
Structural instability tuning as a regulatory mechanism in protein-protein interactions.
Mol.Cell, 44:734-744, 2011

PubMed Abstract: Protein-protein interactions mediate a vast number of cellular processes. Here, we present a regulatory mechanism in protein-protein interactions mediated by finely tuned structural instability and coupled with molecular mimicry. We show that a set of type III secretion (TTS) autoinhibited homodimeric chaperones adopt a molten globule-like state that transiently exposes the substrate binding site as a means to become rapidly poised for binding to their cognate protein substrates. Packing defects at the homodimeric interface stimulate binding, whereas correction of these defects results in less labile chaperones that give rise to nonfunctional biological systems. The protein substrates use structural mimicry to offset the weak spots in the chaperones and to counteract their autoinhibitory conformation. This regulatory mechanism of protein activity is evolutionarily conserved among several TSS systems and presents a lucid example of functional advantage conferred upon a biological system by finely tuned structural instability.

PubMed: 22152477
DOI: 10.1016/j.molcel.2011.09.022

実験手法

SOLUTION NMR