1UK5

Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3

Summary for 1UK5

• Entry DOI: 10.2210/pdb1uk5/pdb
• Descriptor: BAG-family molecular chaperone regulator-3 (1 entity in total)
• Functional Keywords: triple helix bandle, cair-1, bis, riken structural genomics/proteomics initiative, rsgi, structural genomics, chaperone
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 11832.29

Authors

Hatta, R.,Yoshida, M.,Hayashi, F.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-08-19, release date: 2004-02-19, Last modification date: 2023-12-27)

Primary citation

Arakawa, A.,Handa, N.,Ohsawa, N.,Shida, M.,Kigawa, T.,Hayashi, F.,Shirouzu, M.,Yokoyama, S.
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
Structure, 18:309-319, 2010

PubMed Abstract: ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.

PubMed: 20223214
DOI: 10.1016/j.str.2010.01.004

Experimental method

SOLUTION NMR