2C7C

FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)

2C7C の概要

• エントリーDOI: 10.2210/pdb2c7c/pdb
• 関連するPDBエントリー: 1AON 1DK7 1DKD 1EGS 1FY9 1FYA 1GR5 1GR6 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7D 2C7E
• EMDBエントリー: 1180
• 分子名称: 60 KDA CHAPERONIN, 10 KDA CHAPERONIN MOLECULE: GROES, PROTEIN CPN10, GROES PROTEIN (2 entities in total)
• 機能のキーワード: atp-binding, chaperone, atomic structure fitting, cell cycle, cell division, chaperonin, nucleotide-binding, phosphorylation
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 874453.62

構造登録者

Ranson, N.A.,Clare, D.K.,Farr, G.W.,Houldershaw, D.,Horwich, A.L.,Saibil, H.R. (登録日: 2005-11-22, 公開日: 2006-01-25, 最終更新日: 2024-05-08)

主引用文献

Ranson, N.A.,Clare, D.K.,Farr, G.W.,Houldershaw, D.,Horwich, A.L.,Saibil, H.R.
Allosteric Signalling of ATP Hydrolysis in Groel-Groes Complexes.
Nat.Struct.Mol.Biol., 13:147-152, 2006

PubMed Abstract: The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.

PubMed: 16429154
DOI: 10.1038/nsmb1046

実験手法

ELECTRON MICROSCOPY (7.7 Å)