2C7E

REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)

「1GR6」から置き換えられました

2C7E の概要

• エントリーDOI: 10.2210/pdb2c7e/pdb
• 関連するPDBエントリー: 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK
• EMDBエントリー: 1047
• 分子名称: 60 KDA CHAPERONIN, POTASSIUM ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: cell cycle, atp-binding, chaperone, chaperonin, d398a, hp60 class, cell division, nucleotide-binding, phosphorylation
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 804631.83

構造登録者

Ranson, N.A.,Farr, G.W.,Roseman, A.M.,Gowen, B.,Fenton, W.A.,Horwich, A.L.,Saibil, H.R. (登録日: 2005-11-22, 公開日: 2006-02-16, 最終更新日: 2024-05-08)

主引用文献

Ranson, N.A.,Farr, G.W.,Roseman, A.M.,Gowen, B.,Fenton, W.A.,Horwich, A.L.,Saibil, H.R.
ATP-Bound States of Groel Captured by Cryo-Electron Microscopy
Cell(Cambridge,Mass.), 107:869-, 2001

PubMed Abstract: The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.

PubMed: 11779463
DOI: 10.1016/S0092-8674(01)00617-1

実験手法

ELECTRON MICROSCOPY (14.9 Å)