PMID:14738756
| Citation |
Mogk, A and Bukau, B (2004) Molecular chaperones: structure of a protein disaggregase. Curr. Biol. 14:R78-80 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/ultrastructure; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/metabolism; Heat-Shock Proteins/ultrastructure; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Protein Structure, Quaternary/physiology; Protein Structure, Tertiary/physiology; Saccharomyces cerevisiae Proteins/metabolism; Thermus thermophilus/metabolism |
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