Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".

Research output: Contribution to journalArticle


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.


Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences


  • RNA, Phosphates: metabolism, Phosphates: chemistry, Peptide Elongation Factor Tu: metabolism, Peptide Elongation Factor Tu: chemistry, Histidine: metabolism, Histidine: chemistry, Guanosine Triphosphate: metabolism, Guanosine Triphosphate: chemistry, Guanosine Triphosphate: analogs & derivatives, GTP Phosphohydrolases: chemistry, GTP Phosphohydrolases: metabolism, Bacterial: chemistry, Bacterial: metabolism, Ribosomal, 23S: chemistry, 23S: metabolism, Transfer, Amino Acyl: metabolism, Ribosomes: metabolism, Water: chemistry
Original languageEnglish
Pages (from-to)37; author reply 37
Issue number6038
Publication statusPublished - 2011
Publication categoryResearch