6N8V
Hsp104DWB open conformation
Summary for 6N8V
| Entry DOI | 10.2210/pdb6n8v/pdb |
| Related | 6N8T 6N8z |
| EMDB information | 0375 0376 0377 8267 |
| Descriptor | Heat shock protein 104, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | hsp104, clpb, protein disaggregase, molecular chaperone, aaa+, atpase, cryo-em, chaperone |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 6 |
| Total formula weight | 599860.15 |
| Authors | |
| Primary citation | Lee, S.,Roh, S.H.,Lee, J.,Sung, N.,Liu, J.,Tsai, F.T.F. Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. Cell Rep, 26:29-36.e3, 2019 Cited by PubMed Abstract: Hsp104 is a ring-forming, ATP-driven molecular machine that recovers functional protein from both stress-denatured and amyloid-forming aggregates. Although Hsp104 shares a common architecture with Clp/Hsp100 protein unfoldases, different and seemingly conflicting 3D structures have been reported. Examining the structure of Hsp104 poses considerable challenges because Hsp104 readily hydrolyzes ATP, whereas ATP analogs can be slowly turned over and are often contaminated with other nucleotide species. Here, we present the single-particle electron cryo-microscopy (cryo-EM) structures of a catalytically inactive Hsp104 variant (Hsp104) in the ATP-bound state determined between 7.7 Å and 9.3 Å resolution. Surprisingly, we observe that the Hsp104 hexamer adopts distinct ring conformations (closed, extended, and open) despite being in the same nucleotide state. The latter underscores the structural plasticity of Hsp104 in solution, with different conformations stabilized by nucleotide binding. Our findings suggest that, in addition to ATP hydrolysis-driven conformational changes, Hsp104 uses stochastic motions to translocate unfolded polypeptides. PubMed: 30605683DOI: 10.1016/j.celrep.2018.12.037 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.3 Å) |
Structure validation
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