1LA1

Gro-EL Fragment (Apical Domain) Comprising Residues 188-379

1LA1 の概要

• エントリーDOI: 10.2210/pdb1la1/pdb
• 関連するPDBエントリー: 1DK7 1KID
• 分子名称: GroEL (2 entities in total)
• 機能のキーワード: molecular chaperone, protein folding, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A6F5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20727.85

構造登録者

Ashcroft, A.E.,Brinker, A.,Coyle, J.E.,Weber, F.,Kaiser, M.,Moroder, L.,Parsons, M.R.,Jager, J.,Hartl, U.F.,Hayer-Hartl, M.,Radford, S.E. (登録日: 2002-03-27, 公開日: 2002-04-03, 最終更新日: 2023-08-16)

主引用文献

Ashcroft, A.E.,Brinker, A.,Coyle, J.E.,Weber, F.,Kaiser, M.,Moroder, L.,Parsons, M.R.,Jager, J.,Hartl, U.F.,Hayer-Hartl, M.,Radford, S.E.
Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies.
J.Biol.Chem., 277:33115-33126, 2002

PubMed Abstract: Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent crystallographic structures of apical domain constructs that show conformational plasticity in helices H and I. Additionally, ESI-MS indicates that apical domain constructs have co-populated conformations at neutral pH. To assess the ability of different apical domain conformers to bind co-chaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied. Analysis of apical domain-peptide complexes by ESI-MS indicates that only the folded or partially folded apical domain conformations form complexes that survive gas phase conditions. Fluorescence binding studies show that the apical domain can fully bind both peptides independently. No competition for binding was observed, suggesting the peptides have distinct apical domain-binding sites. Blocking the GroES-apical domain-binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least partially, distinct binding sites even in the intact GroEL tetradecamer.

PubMed: 12065585
DOI: 10.1074/jbc.M203398200

実験手法

X-RAY DIFFRACTION (2.06 Å)