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] [DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332]
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 crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.,Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J Science. 1997 Apr 18;276(5311):431-5. PMID:9103205[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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 1997 Apr 18;276(5311):431-5. PMID:9103205
