2LGW

Solution Structure of the J Domain of HSJ1a

Summary for 2LGW

• Entry DOI: 10.2210/pdb2lgw/pdb
• Related: 2LMG
• NMR Information: BMRB: 17825
• Descriptor: DnaJ homolog subfamily B member 2 (1 entity in total)
• Functional Keywords: j domain, hsj1a, co-chaperon, chaperone
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 11297.48

Authors

Zhou, C.,Gao, X.,Cao, C.,Hu, H. (deposition date: 2011-08-02, release date: 2012-01-11, Last modification date: 2024-05-15)

Primary citation

Gao, X.C.,Zhou, C.J.,Zhou, Z.R.,Wu, M.,Cao, C.Y.,Hu, H.Y.
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.
J.Biol.Chem., 287:6044-6052, 2012

PubMed Abstract: The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding β-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical α-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones.

PubMed: 22219199
DOI: 10.1074/jbc.M111.294728

Experimental method

SOLUTION NMR