Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out?
Independent cryo electron microscopy (cryo-EM) studies of the closely related protein disaggregases ClpB and Hsp104 have resulted in two different models of subunit arrangement in the active hexamer. We compare the EM maps and resulting atomic structure fits, discuss their differences, and relate them to published experimental information in an attempt to discriminate between models. In addition, we present some general assessment criteria for low-resolution cryo-EM maps to offer non-structural biologists tools to evaluate these structures.
Department of Crystallography, Birkbeck College, Malet St., London WC1E 7HX, UK.
Petra
P
Wendler
Helen R
HR
Saibil
D020285:Cryoelectron Microscopy / Q000379:methods*; D049071:Endopeptidase Clp; D029968:Escherichia coli Proteins / Q000648:ultrastructure*; D006360:Heat-Shock Proteins / Q000648:ultrastructure*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000648:ultrastructure; D010940:Plant Proteins / Q000648:ultrastructure*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000648:ultrastructure*; D014157:Transcription Factors / Q000648:ultrastructure*
D029968:Escherichia coli Proteins; C115569:HSP101 protein, plant; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C070972:HsP104 protein, S cerevisiae; D049071:Endopeptidase Clp; C069775:ClpB protein, E coli