3KFE

Crystal structures of a group II chaperonin from Methanococcus maripaludis

3KFE の概要

• エントリーDOI: 10.2210/pdb3kfe/pdb
• 関連するPDBエントリー: 3KFB 3KFK
• 分子名称: Chaperonin, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: double homo-octameric rings, atp-binding, chaperone, nucleotide-binding
• 由来する生物種: Methanococcus maripaludis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 449293.65

構造登録者

Pereira, J.H.,Ralston, C.Y.,Douglas, N.,Meyer, D.,Knee, K.M.,Goulet, D.R.,King, J.A.,Frydman, J.,Adams, P.D. (登録日: 2009-10-27, 公開日: 2010-06-23, 最終更新日: 2024-10-30)

主引用文献

Pereira, J.H.,Ralston, C.Y.,Douglas, N.R.,Meyer, D.,Knee, K.M.,Goulet, D.R.,King, J.A.,Frydman, J.,Adams, P.D.
Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
J.Biol.Chem., 285:27958-27966, 2010

PubMed Abstract: Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we describe the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. In contrast with group I chaperonins, in which the equatorial domains share a similar conformation between the open and closed states and the largest motions occurs at the intermediate and apical domains, the three domains of the archaeal chaperonin subunit reorient as a single rigid body. The large rotation observed from the open state to the closed state results in a 65% decrease of the folding chamber volume and creates a highly hydrophilic surface inside the cage. These results suggest a completely distinct closing mechanism in the group II chaperonins as compared with the group I chaperonins.

PubMed: 20573955
DOI: 10.1074/jbc.M110.125344

実験手法

X-RAY DIFFRACTION (3.5 Å)