4V81

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

これはPDB形式変換不可エントリーです。

4V81 の概要

• エントリーDOI: 10.2210/pdb4v81/pdb
• 分子名称: T-complex protein 1 subunit alpha, BERYLLIUM TRIFLUORIDE ION, SULFATE ION, ... (12 entities in total)
• 機能のキーワード: hsp60, eukaryotic chaperonin, actin/tubulin binding, hexadecamer, chaperone
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• 細胞内の位置: Cytoplasm: P12612 P39076 P39077 P39078 P40413 P39079 P42943 P47079
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 1948782.30

構造登録者

Dekker, C.,Roe, S.M.,McCormack, E.A.,Beuron, F.,Pearl, L.H.,Willison, K.R. (登録日: 2010-10-17, 公開日: 2014-07-09, 最終更新日: 2023-09-20)

主引用文献

Dekker, C.,Roe, S.M.,McCormack, E.A.,Beuron, F.,Pearl, L.H.,Willison, K.R.
The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Embo J., 30:3078-3090, 2011

PubMed Abstract: The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essential for eukaryotic life. The CCT interactome shows involvement in folding and assembly of a small range of proteins linked to essential cellular processes such as cytoskeleton assembly and cell-cycle regulation. CCT has a classic chaperonin architecture, with two heterogeneous 8-membered rings stacked back-to-back, enclosing a folding cavity. However, the mechanism by which CCT assists folding is distinct from other chaperonins, with no hydrophobic wall lining a potential Anfinsen cage, and a sequential rather than concerted ATP hydrolysis mechanism. We have solved the crystal structure of yeast CCT in complex with actin at 3.8 Å resolution, revealing the subunit organisation and the location of discrete patches of co-evolving 'signature residues' that mediate specific interactions between CCT and its substrates. The intrinsic asymmetry is revealed by the structural individuality of the CCT subunits, which display unique configurations, substrate binding properties, ATP-binding heterogeneity and subunit-subunit interactions. The location of the evolutionarily conserved N-terminus of Cct5 on the outside of the barrel, confirmed by mutational studies, is unique to eukaryotic cytosolic chaperonins.

PubMed: 21701561
DOI: 10.1038/emboj.2011.208

実験手法

X-RAY DIFFRACTION (3.8 Å)