3a6m | pdb_00003a6m
Crystal structure of GrpE from Thermus thermophilus HB8
Template:ABSTRACT PUBMED 20036249
Function
[GRPE_THET8] 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 (By similarity).
About this Structure
3a6m is a 2 chain structure with sequence from Thet8. Full crystallographic information is available from OCA.
Reference
- Nakamura A, Takumi K, Miki K. Crystal structure of a thermophilic GrpE protein: insight into thermosensing function for the DnaK chaperone system. J Mol Biol. 2010 Mar 5;396(4):1000-11. Epub 2009 Dec 28. PMID:20036249 doi:10.1016/j.jmb.2009.12.028
