1UGO
Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5
Summary for 1UGO
| Entry DOI | 10.2210/pdb1ugo/pdb |
| Descriptor | Bcl2-associated athanogene 5 (1 entity in total) |
| Functional Keywords | triple helix bundle, riken structural genomics/proteomics initiative, rsgi, structural genomics, chaperone |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 10904.05 |
| Authors | Endoh, H.,Hayashi, F.,Seimiya, K.,Shirouzu, M.,Terada, T.,Kigawa, T.,Inoue, M.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Hirota, H.,Yoshida, M.,Tanaka, A.,Osanai, T.,Arakawa, T.,Carninci, P.,Kawai, J.,Hayashizaki, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-06-17, release date: 2004-08-03, 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 Cited by 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: 20223214DOI: 10.1016/j.str.2010.01.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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