4J7Z

Thermus thermophilus DNAJ J- and G/F-DOMAINS

4J7Z の概要

• エントリーDOI: 10.2210/pdb4j7z/pdb
• 関連するPDBエントリー: 4J80
• 分子名称: Chaperone protein DnaJ 2, GLYCEROL (3 entities in total)
• 機能のキーワード: j-domain, polyproline-ii helix, chaperone, dna replication, stress response
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm (By similarity): Q56237
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 77797.98

構造登録者

Barends, T.R.M.,Brosi, R.W.,Steinmetz, A.,Scherer, A.,Hartmann, E.,Eschenbach, J.,Lorenz, T.,Seidel, R.,Shoeman, R.,Zimmermann, S.,Bittl, R.,Schlichting, I.,Reinstein, J. (登録日: 2013-02-14, 公開日: 2013-07-31, 最終更新日: 2024-02-28)

主引用文献

Barends, T.R.,Brosi, R.W.,Steinmetz, A.,Scherer, A.,Hartmann, E.,Eschenbach, J.,Lorenz, T.,Seidel, R.,Shoeman, R.L.,Zimmermann, S.,Bittl, R.,Schlichting, I.,Reinstein, J.
Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ.
Acta Crystallogr.,Sect.D, 69:1540-1552, 2013

PubMed Abstract: Hsp70 chaperones assist in a large variety of protein-folding processes in the cell. Crucial for these activities is the regulation of Hsp70 by Hsp40 cochaperones. DnaJ, the bacterial homologue of Hsp40, stimulates ATP hydrolysis by DnaK (Hsp70) and thus mediates capture of substrate protein, but is also known to possess chaperone activity of its own. The first structure of a complete functional dimeric DnaJ was determined and the mobility of its individual domains in solution was investigated. Crystal structures of the complete molecular cochaperone DnaJ from Thermus thermophilus comprising the J, GF and C-terminal domains and of the J and GF domains alone showed an ordered GF domain interacting with the J domain. Structure-based EPR spin-labelling studies as well as cross-linking results showed the existence of multiple states of DnaJ in solution with different arrangements of the various domains, which has implications for the function of DnaJ.

PubMed: 23897477
DOI: 10.1107/S0907444913010640

実験手法

EPR
X-RAY DIFFRACTION (1.64 Å)