Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ

@inproceedings{Barends2013CombiningCA,
  title={Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ},
  author={Thomas Reinier Barends and Richard W. W. Brosi and Andrea Steinmetz and Anna Scherer and Elisabeth Hartmann and Jessica Eschenbach and Thorsten Lorenz and R. Pfeifle H.-P. Seidel and Robert L. Shoeman and Sabine Zimmermann and Robert Bittl and Ilme Schlichting and Jochen Reinstein},
  booktitle={Acta crystallographica. Section D, Biological crystallography},
  year={2013}
}
Hsp70 chaperones assist in a large variety of protein-folding processes in the cell. Crucial for these activities is the regulation of Hsp70 by Hsp40 cochaperones. DnaJ, the bacterial homologue of Hsp40, stimulates ATP hydrolysis by DnaK (Hsp70) and thus mediates capture of substrate protein, but is also known to possess chaperone activity of its own. The first structure of a complete functional dimeric DnaJ was determined and the mobility of its individual domains in solution was investigated… CONTINUE READING
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