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

被引：28

作者：

Barends, Thomas R. M. ^{[1
]}

Brosi, Richard W. W. ^{[2
]}

Steinmetz, Andrea ^{[1
]}

Scherer, Anna ^{[1
]}

Hartmann, Elisabeth ^{[1
]}

Eschenbach, Jessica ^{[1
]}

Lorenz, Thorsten ^{[1
]}

Seidel, Ralf ^{[3
]}

Shoeman, Robert L. ^{[1
]}

Zimmermann, Sabine ^{[1
]}

Bittl, Robert ^{[2
]}

Schlichting, Ilme ^{[1
]}

Reinstein, Jochen ^{[1
]}

机构：

[1] MPI Med Res, Heidelberg, Germany

[2] Free Univ Berlin, Dept Phys, Berlin, Germany

[3] MPI Mol Physiol, Dortmund, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2013年 / 69卷

关键词：

ESCHERICHIA-COLI DNAJ; PEPTIDE-BINDING FRAGMENT; COMPREHENSIVE SOFTWARE PACKAGE; AUTOMATED STRUCTURE SOLUTION; SITE-DIRECTED MUTAGENESIS; HSP70; COMPLEX-MODELS; HEAT-SHOCK PROTEINS; THERMUS-THERMOPHILUS; J-DOMAIN; CHAPERONE SYSTEM;

D O I：

10.1107/S0907444913010640

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1540 / 1552

页数：13

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