4V4O

Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus

これはPDB形式変換不可エントリーです。

4V4O の概要

• エントリーDOI: 10.2210/pdb4v4o/pdb
• 分子名称: cpn60(GroEL), cpn10(GroES), MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: chaperonin, chaperone, groel, groes, cpn60, cpn10, hsp60, hsp10, folding, adp, atp
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm : P61490 P61492
• タンパク質・核酸の鎖数: 42
• 化学式量合計: 1782769.79

構造登録者

Shimamura, T.,Koike-Takeshita, A.,Yokoyama, K.,Masui, R.,Murai, N.,Yoshida, M.,Taguchi, H.,Iwata, S. (登録日: 2004-05-23, 公開日: 2014-07-09, 最終更新日: 2024-03-20)

主引用文献

Shimamura, T.,Koike-Takeshita, A.,Yokoyama, K.,Masui, R.,Murai, N.,Yoshida, M.,Taguchi, H.,Iwata, S.
Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
STRUCTURE, 12:1471-1480, 2004

PubMed Abstract: The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.

PubMed: 15296740
DOI: 10.1016/j.str.2004.05.020

実験手法

X-RAY DIFFRACTION (2.8 Å)