Published July 1, 2011
| public
Journal Article
Response to Comment on "The Mechanism for Activation of GTP Hydrolysis on the Ribosome"
Chicago
Abstract
Our report of the crystal structure of elongation factor Tu (EF-Tu) and aminoacyl–transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog included a proposed mechanism of GTP hydrolysis by EF-Tu involving histidine-84. Liljas et al. summarize experimental evidence against this mechanism and propose a substrate-assisted catalytic model. However, these experiments and the model are also problematic. Further study is required to definitively determine the mechanism of GTP hydrolysis by EF-Tu.
Additional Information
© 2011 American Association for the Advancement of Science. Received 28 January 2011; accepted 1 June 2011.Additional details
- Eprint ID
- 85186
- DOI
- 10.1126/science.1202532
- Resolver ID
- CaltechAUTHORS:20180308-065659230
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2018-03-08Created from EPrint's datestamp field
- Updated
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2023-02-28Created from EPrint's last_modified field