4J7Z
Thermus thermophilus DNAJ J- and G/F-DOMAINS
Summary for 4J7Z
Entry DOI | 10.2210/pdb4j7z/pdb |
Related | 4J80 |
Descriptor | Chaperone protein DnaJ 2, GLYCEROL (3 entities in total) |
Functional Keywords | j-domain, polyproline-ii helix, chaperone, dna replication, stress response |
Biological source | Thermus thermophilus |
Cellular location | Cytoplasm (By similarity): Q56237 |
Total number of polymer chains | 6 |
Total formula weight | 77797.98 |
Authors | 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. (deposition date: 2013-02-14, release date: 2013-07-31, Last modification date: 2024-02-28) |
Primary citation | 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 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: 23897477DOI: 10.1107/S0907444913010640 PDB entries with the same primary citation |
Experimental method | EPR X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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