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

Liljas, Anders LU ; Ehrenberg, Måns and Åqvist, Johan (2011) In Science 333(6038). p.37-37
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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publication status
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subject
keywords
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
in
Science
volume
333
issue
6038
pages
37 - 37
publisher
American Association for the Advancement of Science (AAAS)
external identifiers
  • pmid:21719661
  • scopus:79959817796
  • pmid:21719661
ISSN
1095-9203
DOI
10.1126/science.1202472
language
English
LU publication?
yes
id
8631d7b6-bcd3-45d8-9ad5-175627d88d21 (old id 2059195)
date added to LUP
2016-04-01 13:44:29
date last changed
2022-01-27 20:48:25
@article{8631d7b6-bcd3-45d8-9ad5-175627d88d21,
  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.}},
  author       = {{Liljas, Anders and Ehrenberg, Måns and Åqvist, Johan}},
  issn         = {{1095-9203}},
  keywords     = {{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}},
  language     = {{eng}},
  number       = {{6038}},
  pages        = {{37--37}},
  publisher    = {{American Association for the Advancement of Science (AAAS)}},
  series       = {{Science}},
  title        = {{Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".}},
  url          = {{http://dx.doi.org/10.1126/science.1202472}},
  doi          = {{10.1126/science.1202472}},
  volume       = {{333}},
  year         = {{2011}},
}