Molecular chaperones: structure of a protein disaggregase.
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.
Mogk
Axel
A
1ZMBH, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany. a.mogk@zmbh.uni-heidelberg.de
Bukau
Bernd
B
D049071:Endopeptidase Clp; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism / Q000648:ultrastructure*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism / Q000648:ultrastructure*; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D020836:Protein Structure, Quaternary / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D016963:Thermus thermophilus / Q000378:metabolism
D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae; D049071:Endopeptidase Clp; C063842:dnaK protein, E coli; C069775:ClpB protein, E coli