Structural highlights
Function
[DNAJ_ECOLI] Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif.
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.,Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874-8. PMID:1826368
- ↑ Zietkiewicz S, Krzewska J, Liberek K. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem. 2004 Oct 22;279(43):44376-83. Epub 2004 Aug 9. PMID:15302880 doi:http://dx.doi.org/10.1074/jbc.M402405200
- ↑ Siegenthaler RK, Grimshaw JP, Christen P. Immediate response of the DnaK molecular chaperone system to heat shock. FEBS Lett. 2004 Mar 26;562(1-3):105-10. PMID:15044009 doi:http://dx.doi.org/10.1016/S0014-5793(04)00190-5
- ↑ Zzaman S, Reddy JM, Bastia D. The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation. J Biol Chem. 2004 Dec 3;279(49):50886-94. Epub 2004 Oct 13. PMID:15485812 doi:http://dx.doi.org/M407531200
- ↑ Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ. Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270 doi:10.1006/jmbi.2000.3923
