1QVR

Crystal Structure Analysis of ClpB

1QVR の概要

• エントリーDOI: 10.2210/pdb1qvr/pdb
• 分子名称: ClpB protein, PLATINUM (II) ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: coiled coil, aaa atpase, chaperone
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm (Probable): Q9RA63
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 296681.43

構造登録者

Lee, S.,Sowa, M.E.,Watanabe, Y.,Sigler, P.B.,Chiu, W.,Yoshida, M.,Tsai, F.T.F. (登録日: 2003-08-28, 公開日: 2003-10-21, 最終更新日: 2024-02-14)

主引用文献

Lee, S.,Sowa, M.E.,Watanabe, Y.,Sigler, P.B.,Chiu, W.,Yoshida, M.,Tsai, F.T.F.
The Structure of ClpB: A Molecular Chaperone that Rescues Proteins from an Aggregated State
Cell(Cambridge,Mass.), 115:229-240, 2003

PubMed Abstract: Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate protein disaggregation. Bacterial ClpB and its eukaryotic homolog Hsp104 are essential proteins of the heat-shock response, which have the remarkable capacity to rescue stress-damaged proteins from an aggregated state. We have determined the structure of Thermus thermophilus ClpB (TClpB) using a combination of X-ray crystallography and cryo-electron microscopy (cryo-EM). Our single-particle reconstruction shows that TClpB forms a two-tiered hexameric ring. The ClpB/Hsp104-linker consists of an 85 A long and mobile coiled coil that is located on the outside of the hexamer. Our mutagenesis and biochemical data show that both the relative position and motion of this coiled coil are critical for chaperone function. Taken together, we propose a mechanism by which an ATP-driven conformational change is coupled to a large coiled-coil motion, which is indispensable for protein disaggregation.

PubMed: 14567920
DOI: 10.1016/S0092-8674(03)00807-9

実験手法

X-RAY DIFFRACTION (3 Å)