7NDX
Crystal structure of the human HSP40 DNAJB1-CTDs in complex with a peptide of NudC
Summary for 7NDX
| Entry DOI | 10.2210/pdb7ndx/pdb |
| Descriptor | DnaJ homolog subfamily B member 1, Nuclear migration protein nudC, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | chaperones, protein complex, chaperone |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 25810.68 |
| Authors | Delhommel, F.,Zak, K.M.,Popowicz, G.M.,Sattler, M. (deposition date: 2021-02-02, release date: 2022-01-19, Last modification date: 2024-01-31) |
| Primary citation | Biebl, M.M.,Delhommel, F.,Faust, O.,Zak, K.M.,Agam, G.,Guo, X.,Muhlhofer, M.,Dahiya, V.,Hillebrand, D.,Popowicz, G.M.,Kampmann, M.,Lamb, D.C.,Rosenzweig, R.,Sattler, M.,Buchner, J. NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems. Mol.Cell, 82:555-, 2022 Cited by PubMed Abstract: In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem with the maturation of a diverse array of client proteins. The transfer of nonnative clients between these systems is essential to the chaperoning process, but how it is regulated is still not clear. We discovered that NudC is an essential transfer factor with an unprecedented mode of action: NudC interacts with Hsp40 in Hsp40-Hsp70-client complexes and displaces Hsp70. Then, the interaction of NudC with Hsp90 allows the direct transfer of Hsp40-bound clients to Hsp90 for further processing. Consistent with this mechanism, NudC increases client activation in vitro as well as in cells and is essential for cellular viability. Together, our results show the complexity of the cooperation between the major chaperone machineries in the eukaryotic cytosol. PubMed: 35063133DOI: 10.1016/j.molcel.2021.12.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.541 Å) |
Structure validation
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