Molecular Chaperones: Structure of a Protein Disaggregase
نویسندگان
چکیده
The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.
منابع مشابه
Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone.
BACKGROUND A novel chaperone, cpSRP43, recognizes and disassembles the aggregates formed by its client proteins. RESULTS The client proteins of cpSRP43 form stable disc-shaped aggregates with the chaperone recognition motif displayed onthe surface. CONCLUSION The surface-exposed motif on the aggregate allows it to be recognized by its chaperone. SIGNIFICANCE Understanding the structure an...
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Cells have evolved a sophisticated proteostasis network to ensure that proteins acquire and retain their native structure and function. Critical components of this network include molecular chaperones and protein disaggregases, which function to prevent and reverse deleterious protein misfolding. Nevertheless, proteostasis networks have limits, which when exceeded can have fatal consequences as...
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The ClpB/Hsp104 and Hsp70 classes of molecular chaperones use ATP hydrolysis to dissociate protein aggregates and complexes, and to move proteins through membranes. ClpB/Hsp104 are members of the AAA+ family of proteins which form ring-shaped hexamers. Loops lining the pore in the ring engage substrate proteins as extended polypeptides. Interdomain rotations and conformational changes in these ...
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عنوان ژورنال:
- Current Biology
دوره 14 شماره
صفحات -
تاریخ انتشار 2004