6533b855fe1ef96bd12b0929
RESEARCH PRODUCT
Energetic aspects of intramolecular coupling between the nucleotide binding site and the distal switch II region of the yeast RAS2 protein
Ottavio FasanoEmmanuele De Vendittissubject
Saccharomyces cerevisiae ProteinsStereochemistryCdc25GuanineSaccharomyces cerevisiaeGlycineBiophysicsSaccharomyces cerevisiaeGuanosine DiphosphateBiochemistryFungal ProteinsStructure-Activity RelationshipSCD25chemistry.chemical_compoundGTP-Binding ProteinsStructural BiologyEscherichia coliSerineGeneticsNucleotideBinding siteRas2Molecular Biologychemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesCDC25biologyGDP bindingTemperatureCell Biologybiology.organism_classificationGuanine NucleotidesRecombinant ProteinsYeastchemistryras ProteinsGDP exchange factorbiology.proteinThermodynamicsRASdescription
AbstractWe have studied the interaction of the yeast RAS2 protein with guanine nucleotides using energetic parameters for the dissociation of RAS·nucleotide complexes. The results indicated that a Gly → Ser substitution at position 82 led to an altered interaction with GppNHp and, to a lesser extent, also with GDP. It was also possible to conclude that structural perturbation of Gly82 can stimulate nucleotide release by decreasing the energetic barrier for nucleotide dissociation. This, together with the observation that residues 80 and 81 are involved in the response of RAS to nucleotide exchange factors without affecting GDP binding per se, suggests a potential mechanism for exchange factor-stimulated GDP release.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1994-06-27 | FEBS Letters |