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• W2022125124 endingPage "162" @default.
• W2022125124 startingPage "157" @default.
• W2022125124 abstract "The modification of E.coli elongation factor Ts (EF-Ts) by NEM and other sulfhydryl reagents inactivates the protein's ability to bind EF-Tu.GDP and to catalyze GDP exchange. The reactive residue was found to be Cys-22. Replacement of Cys-22 by Ser or Gly only partially impairs the binding or catalytic properties of EF-Ts while it completely protects EF-Ts from the inactivation by NEM. Cys-22 of EF-Ts is not located at the EF-Ts.EF-Tu interface, yet it can be modified only when EF-Ts is not bound to EF-Tu. These results support the proposal that the conformation change around Cys-22 in the amino terminus of EF-Ts rather than Cys-22 itself is essential for binding EF-Tu. Apparently, modification of Cys-22 by NEM disrupts the conformation change and inactivates EF-Ts. The return of EF-Ts to its native conformation may provide the driving force for the rate-determining step in the catalytic cycle, the dissociation of EF-Ts from EF-Tu.GNP." @default.
• W2022125124 created "2016-06-24" @default.
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• W2022125124 date "1997-12-01" @default.
• W2022125124 modified "2023-09-25" @default.
• W2022125124 title "The Role of Cysteinyl Residues in the Activity of Bacterial Elongation Factor Ts, a Guanosine Nucleotide Dissociation Protein" @default.
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• W2022125124 doi "https://doi.org/10.1006/abbi.1997.0375" @default.
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