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

Barends, Thomas; Brosi, R. W. W.; Steinmetz, Andrea; Scherer, Anna; Hartmann, Elisabeth; Eschenbach, Jessica; Lorenz, Thorsten; Seidel, R.; Shoeman, Robert L.; Zimmermann, Sabine; Bittl, R.; Schlichting, Ilme; Reinstein, Jochen

doi:10.1107/S0907444913010640

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

MPS-Authors

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Barends, Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117902

Steinmetz, Andrea
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95158

Scherer, Anna
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117815

Hartmann, Elisabeth
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117872

Eschenbach, Jessica
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117931

Lorenz, Thorsten
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117689

Zimmermann, Sabine
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein, Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://journals.iucr.org/d/issues/2013/08/00/mh5089/mh5089.pdf
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http://dx.doi.org/10.1107/S0907444913010640
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Citation

Barends, T., Brosi, R. W. W., Steinmetz, A., Scherer, A., Hartmann, E., Eschenbach, J., et al. (2013). Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 69(8), 1540-1552. doi:10.1107/S0907444913010640.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-8FE6-1

Abstract

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. Crystal structures of the complete molecular cochaperone DnaJ from Thermus thermophilus comprising the J, GF and C-terminal domains and of the J and GF domains alone showed an ordered GF domain interacting with the J domain. Structure-based EPR spin-labelling studies as well as cross-linking results showed the existence of multiple states of DnaJ in solution with different arrangements of the various domains, which has implications for the function of DnaJ.