5NRO

Structure of full-length DnaK with bound J-domain

Summary for 5NRO

• Entry DOI: 10.2210/pdb5nro/pdb
• Descriptor: Chaperone protein DnaK, Chaperone protein DnaJ, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: dnak, dnaj, chaperone, hsp70, hsp40
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P0A6Y8 P08622
• Total number of polymer chains: 2
• Total formula weight: 78843.51

Authors

Kopp, J.,Kityk, R.,Mayer, M.P. (deposition date: 2017-04-25, release date: 2018-01-17, Last modification date: 2024-11-06)

Primary citation

Kityk, R.,Kopp, J.,Mayer, M.P.
Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones.
Mol. Cell, 69:227-237.e4, 2018

PubMed Abstract: Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and concomitant substrate trapping. We present the crystal structure of the J-domain of Escherichia coli DnaJ in complex with the E. coli Hsp70 DnaK. The J-domain interacts not only with DnaK's nucleotide-binding domain (NBD) but also with its substrate-binding domain (SBD) and packs against the highly conserved interdomain linker. Mutational replacement of contacts between J-domain and SBD strongly reduces the ability of substrates to stimulate ATP hydrolysis in the presence of DnaJ and compromises viability at heat shock temperatures. Our data demonstrate that the J-domain and the substrate do not deliver completely independent signals for ATP hydrolysis, but the J-domain, in addition to its direct influence on Hsp70s catalytic center, makes Hsp70 more responsive for the hydrolysis-inducing signal of the substrate, resulting in efficient substrate trapping.

PubMed: 29290615
DOI: 10.1016/j.molcel.2017.12.003

Experimental method

X-RAY DIFFRACTION (3.25 Å)