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-Structure paper
タイトル | Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. |
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ジャーナル・号・ページ | Cell Rep, Vol. 26, Issue 1, Page 29-36.e3, Year 2019 |
掲載日 | 2019年1月2日 |
![]() | Sukyeong Lee / Soung Hun Roh / Jungsoon Lee / Nuri Sung / Jun Liu / Francis T F Tsai / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 7.7 - 9.3 Å |
構造データ | |
化合物 | ![]() ChemComp-ATP: |
由来 |
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![]() | CHAPERONE / Hsp104 / ClpB / protein disaggregase / molecular chaperone / AAA+ / ATPase / cryo-EM |