1GRL

THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS

1GRL の概要

• エントリーDOI: 10.2210/pdb1grl/pdb
• 分子名称: GROEL (HSP60 CLASS) (1 entity in total)
• 機能のキーワード: chaperonin
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 400942.72

構造登録者

Braig, K.,Otwinowski, Z.,Hegde, R.,Boisvert, D.C.,Joachimiak, A.,Horwich, A.L.,Sigler, P.B. (登録日: 1995-03-07, 公開日: 1995-10-15, 最終更新日: 2024-02-07)

主引用文献

Braig, K.,Otwinowski, Z.,Hegde, R.,Boisvert, D.C.,Joachimiak, A.,Horwich, A.L.,Sigler, P.B.
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Nature, 371:578-586, 1994

PubMed Abstract: The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.

PubMed: 7935790
DOI: 10.1038/371578a0

実験手法

X-RAY DIFFRACTION (2.8 Å)