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3a6m
From Proteopedia
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{{STRUCTURE_3a6m| PDB=3a6m | SCENE= }} | {{STRUCTURE_3a6m| PDB=3a6m | SCENE= }} | ||
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===Crystal structure of GrpE from Thermus thermophilus HB8=== | ===Crystal structure of GrpE from Thermus thermophilus HB8=== | ||
| + | {{ABSTRACT_PUBMED_20036249}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/GRPE_THET8 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== | ==About this Structure== | ||
| - | [[3a6m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3a6m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6M OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:020036249</ref><references group="xtra"/> | + | <ref group="xtra">PMID:020036249</ref><references group="xtra"/><references/> |
| - | [[Category: | + | [[Category: Thet8]] |
[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Nakamura, A.]] | [[Category: Nakamura, A.]] | ||
Revision as of 06:29, 22 January 2014
Contents |
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
Categories: Thet8 | Miki, K. | Nakamura, A. | Takumi, K. | Chaperone | Coiled-coil | Dimer | Four-helix bundle | Grpe | Stress response
