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          Institute: MPI für medizinische Forschung     Collection: Jahbruch 2014_archival     Display Documents



ID: 681455.0, MPI für medizinische Forschung / Jahbruch 2014_archival
Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ
Translation of Title:Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ
Authors:Barends, Thomas; Brosi, Richard W. W.; Steinmetz, Andrea; Scherer, Anna; Hartmann, Elisabeth; Eschenbach, Jessica; Lorenz, Thorsten; Seidel, Ralf; Shoeman, Robert L.; Zimmermann, Sabine; Bittl, Robert; Schlichting, Ilme; Reinstein, Jochen
Language:English
Date of Publication (YYYY-MM-DD):2013-08-01
Title of Journal:Acta Crystallographica D
Journal Abbrev.:Acta Crystallogr. Sec. D
Volume:69
Issue / Number:8
Start Page:1540
End Page:1552
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
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
External Publication Status:published
Document Type:Article
Communicated by:wkaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Analytical Protein Biochemistry
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Coherent diffractive imaging
Identifiers:LOCALID:7915
URI:http%3A%2F%2Fjournals.iucr.org%2Fd%2Fissues%2F2013...
URI:http%3A%2F%2Fjournals.iucr.org%2Fd%2Fissues%2F2013...
URI:http%3A%2F%2Fscripts.iucr.org%2Fcgi-bin%2Fpaper%3F...
DOI:10.1107%2FS0907444913010640
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