8K2R
The structure of HtpG M domain in complex with unstructured D131D binding site b
Summary for 8K2R
| Entry DOI | 10.2210/pdb8k2r/pdb |
| Descriptor | Molecular chaperone HtpG (Fragment), Disordered protein(D131D) (2 entities in total) |
| Functional Keywords | e.coli hsp90, chaperone |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 40148.50 |
| Authors | |
| Primary citation | Qu, X.,Zhao, S.,Wan, C.,Zhu, L.,Ji, T.,Rossi, P.,Wang, J.,Kalodimos, C.G.,Wang, C.,Xu, W.,Huang, C. Structural basis for the dynamic chaperoning of disordered clients by Hsp90. Nat.Struct.Mol.Biol., 31:1482-1491, 2024 Cited by PubMed Abstract: Molecular chaperone heat shock protein 90 (Hsp90) is a ubiquitous regulator that fine-tunes and remodels diverse client proteins, exerting profound effects on normal biology and diseases. Unraveling the mechanistic details of Hsp90's function requires atomic-level insights into its client interactions throughout the adenosine triphosphate-coupled functional cycle. However, the structural details of the initial encounter complex in the chaperone cycle, wherein Hsp90 adopts an open conformation while engaging with the client, remain elusive. Here, using nuclear magnetic resonance spectroscopy, we determined the solution structure of Hsp90 in its open state, bound to a disordered client. Our findings reveal that Hsp90 uses two distinct binding sites, collaborating synergistically to capture discrete hydrophobic segments within client proteins. This bipartite interaction generates a versatile complex that facilitates rapid conformational sampling. Moreover, our investigations spanning various clients and Hsp90 orthologs demonstrate a pervasive mechanism used by Hsp90 orthologs to accommodate the vast array of client proteins. Collectively, our work contributes to establish a unified conceptual and mechanistic framework, elucidating the intricate interplay between Hsp90 and its clients. PubMed: 38890550DOI: 10.1038/s41594-024-01337-z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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