1dkg

Structural highlights

Function

GRPE_ECOLI Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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.

See Also

• Heat Shock Protein structures

References

1. ↑ 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
2. ↑ Wu B, Wawrzynow A, Zylicz M, Georgopoulos C. Structure-function analysis of the Escherichia coli GrpE heat shock protein. EMBO J. 1996 Sep 16;15(18):4806-16. PMID:8890154
3. ↑ Mehl AF, Heskett LD, Neal KM. A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK. Biochem Biophys Res Commun. 2001 Mar 30;282(2):562-9. PMID:11401497 doi:http://dx.doi.org/10.1006/bbrc.2001.4567
4. ↑ Brehmer D, Gassler C, Rist W, Mayer MP, Bukau B. Influence of GrpE on DnaK-substrate interactions. J Biol Chem. 2004 Jul 2;279(27):27957-64. Epub 2004 Apr 21. PMID:15102842 doi:http://dx.doi.org/10.1074/jbc.M403558200