1A6D

THERMOSOME FROM T. ACIDOPHILUM

1A6D の概要

• エントリーDOI: 10.2210/pdb1a6d/pdb
• 分子名称: THERMOSOME (ALPHA SUBUNIT), THERMOSOME (BETA SUBUNIT) (2 entities in total)
• 機能のキーワード: thermoplasma acidophilum, group ii chaperonin, cct, tric, protein folding, atpase, chaperonin
• 由来する生物種: Thermoplasma acidophilum; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116876.45

構造登録者

Ditzel, L.,Loewe, J.,Stock, D.,Stetter, K.-O.,Huber, H.,Huber, R.,Steinbacher, S. (登録日: 1998-02-24, 公開日: 1999-03-23, 最終更新日: 2024-02-07)

主引用文献

Ditzel, L.,Lowe, J.,Stock, D.,Stetter, K.O.,Huber, H.,Huber, R.,Steinbacher, S.
Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.
Cell(Cambridge,Mass.), 93:125-138, 1998

PubMed Abstract: We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.

PubMed: 9546398
DOI: 10.1016/S0092-8674(00)81152-6

実験手法

X-RAY DIFFRACTION (2.6 Å)