1JON

GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345

1JON の概要

• エントリーDOI: 10.2210/pdb1jon/pdb
• 分子名称: GROEL, HSP60 CLASS (2 entities in total)
• 機能のキーワード: chaperone, cell division, atp-binding, phosphorylation
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6F5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16642.24

構造登録者

Buckle, A.M.,Fersht, A.R. (登録日: 1996-05-30, 公開日: 1997-03-12, 最終更新日: 2024-05-22)

主引用文献

Zahn, R.,Buckle, A.M.,Perrett, S.,Johnson, C.M.,Corrales, F.J.,Golbik, R.,Fersht, A.R.
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
Proc.Natl.Acad.Sci.USA, 93:15024-15029, 1996

PubMed Abstract: The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.

PubMed: 8986757
DOI: 10.1073/pnas.93.26.15024

実験手法

X-RAY DIFFRACTION (2.5 Å)