1YUW

crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant

1YUW の概要

• エントリーDOI: 10.2210/pdb1yuw/pdb
• 関連するPDBエントリー: 3HSC 7HSC
• 分子名称: Heat shock cognate 71 kDa protein (2 entities in total)
• 機能のキーワード: chaperone
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm : P19120
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60978.87

構造登録者

Jiang, J.,Lafer, E.M.,Prasad, K.,Sousa, R. (登録日: 2005-02-14, 公開日: 2005-10-04, 最終更新日: 2024-02-14)

主引用文献

Jiang, J.,Prasad, K.,Lafer, E.M.,Sousa, R.
Structural basis of interdomain communication in the Hsc70 chaperone
Mol.Cell, 20:513-524, 2005

PubMed Abstract: Hsp70 family proteins are highly conserved chaperones involved in protein folding, degradation, targeting and translocation, and protein complex remodeling. They are comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding to the NBD alters SBD conformation and substrate binding kinetics, but an understanding of the mechanism of interdomain communication has been hampered by the lack of a crystal structure of an intact chaperone. We report here the 2.6 angstroms structure of a functionally intact bovine Hsc70 (bHsc70) and a mutational analysis of the observed interdomain interface and the immediately adjacent interdomain linker. This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the interdomain linker invades and disrupts the interdomain interface when ATP binds.

PubMed: 16307916
DOI: 10.1016/j.molcel.2005.09.028

実験手法

X-RAY DIFFRACTION (2.6 Å)