title: Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".
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.
authors: Department of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden. anders.liljas@biochemistry.lu.se
authors: Anders
authors: A
authors: Liljas
authors: Måns
authors: M
authors: Ehrenberg
authors: Johan
authors: J
authors: Åqvist
mesh_terms: D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism*; D010710:Phosphates / Q000737:chemistry / Q000378:metabolism; D011522:Protons; D012329:RNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D012338:RNA, Ribosomal, 23S / Q000737:chemistry / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D014867:Water / Q000737:chemistry
chemical_list: D010710:Phosphates; D011522:Protons; D012329:RNA, Bacterial; D012338:RNA, Ribosomal, 23S; D012346:RNA, Transfer, Amino Acyl; D014867:Water; C011265:guanosine 5'-(beta,gamma-methylene)triphosphate; D006639:Histidine; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases; D010444:Peptide Elongation Factor Tu