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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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organization
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Contribution to journal
publication status
published
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
The American Association for the Advancement of Science
external identifiers
  • pmid:21719661
  • scopus:79959817796
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
2011-10-03 12:47:14
date last changed
2017-01-01 05:51:08
@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},
  keyword      = {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    = {The American Association for the Advancement of Science},
  series       = {Science},
  title        = {Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".},
  url          = {http://dx.doi.org/10.1126/science.1202472},
  volume       = {333},
  year         = {2011},
}