Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2059195
- author
- Liljas, Anders LU ; Ehrenberg, Måns and Åqvist, Johan
- organization
- publishing date
- 2011
- type
- 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
- 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}}, }