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Updated: May 31, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
Comment on "The mechanism for activation of GTP hydrolysis on the ribosome"
Anders Liljas1, Måns Ehrenberg, Johan Åqvist
1Department of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden. anders.liljas@biochemistry.lu.se
Abstract:
Voorhees et al. (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. However, their identification of histidine-84 of EF-Tu as deprotonating the catalytic water molecule is problematic in relation to their atomic structure; the terminal phosphate of GTP is more likely to be the proper proton acceptor.
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