PMID:12368105
| Citation |
Gelinas, AD, Langsetmo, K, Toth, J, Bethoney, KA, Stafford, WF and Harrison, CJ (2002) A structure-based interpretation of E.coli GrpE thermodynamic properties. J. Mol. Biol. 323:131-42 |
|---|---|
| Abstract |
GrpE is the nucleotide exchange factor for the Escherichia coli molecular chaperone DnaK, the prokaryotic homologue of Hsp70. Thermodynamic properties of GrpE structural domains were characterized by examining a number of structural and point mutants using circular dichroism, differential scanning calorimetry and analytical ultracentrifugation. These structural domains are the long paired N-terminal helices, the central four-helix bundle, and the C-terminal compact beta-domains. We show that the central four-helix bundle (t(m) approximately 75 degrees C) provides a stable platform for the association of the long paired N-terminal helices (t(m) approximately 50 degrees C), which can then function as a temperature sensor. The stability of the N-terminal helices is linked to the presence of the C-terminal compact beta-domains of GrpE, providing a potential mechanism for coupling of DnaK-binding activity of GrpE with temperature. On the basis of our thermodynamic analysis of E.coli GrpE, we present a structure-based model for the melting properties of the nucleotide exchange factor, wherein the long paired helices function as a molecular thermocouple. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Circular Dichroism; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins; Heat-Shock Proteins/chemistry; Protein Structure, Secondary; Thermodynamics |
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