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

Science. 2011 Jul 1;333(6038):37; author reply 37. doi: 10.1126/science.1202472.

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.

Publication types

  • Comment

MeSH terms

  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism
  • Guanosine Triphosphate / analogs & derivatives*
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism*
  • Histidine / chemistry
  • Histidine / metabolism
  • Hydrogen Bonding
  • Hydrolysis
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Peptide Elongation Factor Tu / chemistry*
  • Peptide Elongation Factor Tu / metabolism*
  • Phosphates / chemistry
  • Phosphates / metabolism
  • Protons
  • RNA, Bacterial / chemistry
  • RNA, Bacterial / metabolism
  • RNA, Ribosomal, 23S / chemistry
  • RNA, Ribosomal, 23S / metabolism
  • RNA, Transfer, Amino Acyl / metabolism
  • Ribosomes / metabolism*
  • Water / chemistry

Substances

  • Phosphates
  • Protons
  • RNA, Bacterial
  • RNA, Ribosomal, 23S
  • RNA, Transfer, Amino Acyl
  • Water
  • guanosine 5'-(beta,gamma-methylene)triphosphate
  • Histidine
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • Peptide Elongation Factor Tu