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• W2029399046 abstract "Many proteins that hydrolyze ATP or GTP have comparable amino acid residues for which specific roles have been proposed in a mechanism for the chemistry of hydrolysis. These roles include polarization by a glutamate residue of a water molecule for the attack on the γ-phosphoryl group of the nucleotide, stabilization of the transition state by an arginine finger, discrimination between bound nucleoside triphosphate and diphosphate by a γ sensor residue, and coordination by an aspartate of the Mg2+ that accompanies the substrate nucleotide. We mutated four candidate residues for these roles in the Escherichia coli transcription termination factor Rho, E211, R366, R212, and D265, and characterized the resulting proteins for oligomerization state, ligand binding, RNA-dependent ATP hydrolysis, and, in rapid mix/chemical quench experiments, achievement of the chemistry step of hydrolysis. All four mutant proteins behaved as expected for Rhos lacking the proposed mechanistic roles. The results provide firm biochemical evidence in support of the proposed model for hydrolysis chemistry." @default.
• W2029399046 created "2016-06-24" @default.
• W2029399046 creator A5041896946 @default.
• W2029399046 creator A5045420710 @default.
• W2029399046 date "2010-12-01" @default.
• W2029399046 modified "2023-10-18" @default.
• W2029399046 title "Evidence for Amino Acid Roles in the Chemistry of ATP Hydrolysis in Escherichia coli Rho" @default.
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• W2029399046 doi "https://doi.org/10.1016/j.jmb.2010.09.039" @default.
• W2029399046 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20950626" @default.
• W2029399046 hasPublicationYear "2010" @default.
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