4LJ5

ClpB NBD2 from T. thermophilus in complex with ADP

4LJ5 の概要

• エントリーDOI: 10.2210/pdb4lj5/pdb
• 関連するPDBエントリー: 4LJ4 4LJ6 4LJ7 4LJ8 4LJ9 4LJA
• 分子名称: Chaperone protein ClpB, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: aaa+ protein, nucleotide binding domain, molecular chaperone, disaggregase, 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: 1
• 化学式量合計: 38785.20

構造登録者

Zeymer, C.,Barends, T.R.M.,Werbeck, N.D.,Schlichting, I.,Reinstein, J. (登録日: 2013-07-04, 公開日: 2014-02-12, 最終更新日: 2023-11-08)

主引用文献

Zeymer, C.,Barends, T.R.M.,Werbeck, N.D.,Schlichting, I.,Reinstein, J.
Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor
Acta Crystallogr.,Sect.D, 70:582-595, 2014

PubMed Abstract: ATPases of the AAA+ superfamily are large oligomeric molecular machines that remodel their substrates by converting the energy from ATP hydrolysis into mechanical force. This study focuses on the molecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cellular stress conditions. Based on high-resolution crystal structures in different nucleotide states, mutational analysis and nucleotide-binding kinetics experiments, the ATPase cycle of the C-terminal nucleotide-binding domain (NBD2), one of the motor subunits of this AAA+ disaggregation machine, is dissected mechanistically. The results provide insights into nucleotide sensing, explaining how the conserved sensor 2 motif contributes to the discrimination between ADP and ATP binding. Furthermore, the role of a conserved active-site arginine (Arg621), which controls binding of the essential Mg2+ ion, is described. Finally, a hypothesis is presented as to how the ATPase activity is regulated by a conformational switch that involves the essential Walker A lysine. In the proposed model, an unusual side-chain conformation of this highly conserved residue stabilizes a catalytically inactive state, thereby avoiding unnecessary ATP hydrolysis.

PubMed: 24531492
DOI: 10.1107/S1399004713030629

実験手法

X-RAY DIFFRACTION (2.4 Å)