Keeping a dangerous molecular machine under control
In Elife, we present the crystal structure of Hsp104 from Chaetomium thermophilum that – although forming a helical filament – reveals important mechanistic features. First, we identify the long-sought mechanical link coupling the two AAA rings of HSP100 chaperones and, second, delineate structural details underlying the regulatory role of the CCD. Jointly, these two elements make Hsp104 a very potent yet highly tunable protein disaggregase.
The Hsp104 team - Alex, Sonja and Marcin
Hsp104 is under control of a "restraint mask" assembled by the CCD. The whole scenario reminds to the shown picture.