1KID

GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET

1KID の概要

• エントリーDOI: 10.2210/pdb1kid/pdb
• 分子名称: GROEL (HSP60 CLASS) (2 entities in total)
• 機能のキーワード: chaperone, hsp60, groel, 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: 22060.32

構造登録者

Buckle, A.M.,Fersht, A.R. (登録日: 1996-12-13, 公開日: 1997-09-17, 最終更新日: 2024-05-22)

主引用文献

Buckle, A.M.,Zahn, R.,Fersht, A.R.
A structural model for GroEL-polypeptide recognition.
Proc.Natl.Acad.Sci.USA, 94:3571-3575, 1997

PubMed Abstract: A monomeric peptide fragment of GroEL, consisting of residues 191-376, is a mini-chaperone with a functional chaperoning activity. We have solved the crystal structure at 1.7 A resolution of GroEL(191-376) with a 17-residue N-terminal tag. The N-terminal tag of one molecule binds in the active site of a neighboring molecule in the crystal. This appears to mimic the binding of a peptide substrate molecule. Seven substrate residues are bound in a relatively extended conformation. Interactions between the substrate and the active site are predominantly hydrophobic, but there are also four hydrogen bonds between the main chain of the substrate and side chains of the active site. Although the preferred conformation of a bound substrate is essentially extended, the flexibility of the active site may allow it to accommodate the binding of exposed hydrophobic surfaces in general, such as molten globule-type structures. GroEL can therefore help unfold proteins by binding to a hydrophobic region and exert a binding pressure toward the fully unfolded state, thus acting as an "unfoldase." The structure of the mini-chaperone is very similar to that of residues 191-376 in intact GroEL, so we can build it into GroEL and reconstruct how a peptide can bind to the tetradecamer. A ring of connected binding sites is noted that can explain many aspects of substrate binding and activity.

PubMed: 9108017
DOI: 10.1073/pnas.94.8.3571

実験手法

X-RAY DIFFRACTION (1.7 Å)