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- W1979195429 abstract "Elongation factor G (EF-G) from Escherichia coli is a large, five-domain GTPase that promotes tRNA translocation on the ribosome. Full activity requires GTP hydrolysis, suggesting that a conformational change of the factor is important for function. To restrict the intramolecular mobility, two cysteine residues were engineered into domains 1 and 5 of EF-G that spontaneously formed a disulfide cross-link. Cross-linked EF-G retained GTPase activity on the ribosome, whereas it was inactive in translocation as well as in turnover. Both activities were restored when the cross-link was reversed by reduction. These results strongly argue against a GTPase switch-type model of EF-G function and demonstrate that conformational mobility is an absolute requirement for EF-G function on the ribosome." @default.
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- W1979195429 date "2000-08-01" @default.
- W1979195429 modified "2023-09-29" @default.
- W1979195429 title "Conformationally Restricted Elongation Factor G Retains GTPase Activity but Is Inactive in Translocation on the Ribosome" @default.
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- W1979195429 doi "https://doi.org/10.1016/s1097-2765(00)00049-6" @default.
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