1DKD

CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX

1DKD の概要

• エントリーDOI: 10.2210/pdb1dkd/pdb
• 関連するPDBエントリー: 1DK7
• 分子名称: GROEL, 12-MER PEPTIDE (3 entities in total)
• 機能のキーワード: molecular chaperon, hsp60, protein folding, peptide selection, phage display, peptide binding groove formed by paired helices substrate peptide in beta-sheet, chaperone
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P0A6F5
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 68759.78

構造登録者

Chen, L.,Sigler, P.B. (登録日: 1999-12-07, 公開日: 2000-01-12, 最終更新日: 2024-02-07)

主引用文献

Chen, L.,Sigler, P.B.
The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity.
Cell(Cambridge,Mass.), 99:757-768, 1999

PubMed Abstract: The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.

PubMed: 10619429
DOI: 10.1016/S0092-8674(00)81673-6

実験手法

X-RAY DIFFRACTION (2.1 Å)