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4J80

Thermus thermophilus DnaJ

Summary for 4J80
Entry DOI10.2210/pdb4j80/pdb
Related4J7Z
DescriptorChaperone protein DnaJ 2 (1 entity in total)
Functional Keywordsmolecular chaperone, thermus thermophilus dnaj2 delta mutant, chaperone
Biological sourceThermus thermophilus
Cellular locationCytoplasm (By similarity): Q56237
Total number of polymer chains4
Total formula weight127264.58
Authors
Primary citationBarends, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
EPR
X-RAY DIFFRACTION (2.9 Å)
Structure validation

238895

数据于2025-07-16公开中

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