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

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.

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Barends, Thomas1, Author              
Brosi, R. W. W., Author
Steinmetz, Andrea1, Author              
Scherer, Anna1, Author              
Hartmann, Elisabeth1, Author              
Eschenbach, Jessica1, Author              
Lorenz, Thorsten1, Author              
Seidel, R., Author
Shoeman, Robert L.1, Author              
Zimmermann, Sabine1, Author              
Bittl, R., Author
Schlichting, Ilme1, Author              
Reinstein, Jochen1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: molecular chaperones; crystal dehydration; radiation-damage-induced phasing with anomalous scattering; single-wavelength anomalous diffraction; electron paramagnetic resonance; cross-linking; hybrid structure determination.
 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.

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Language(s): eng - English
 Dates: 2013-02-142013-04-182013-07-192013-02-14
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0907444913010640
Other: 7915
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Title: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Other : Acta Crystallogr D
Source Genre: Journal
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Pages: - Volume / Issue: 69 (8) Sequence Number: - Start / End Page: 1540 - 1552 Identifier: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619