Publication Date:
2011-07-02
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liljas, Anders -- Ehrenberg, Mans -- Aqvist, Johan -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):37; author reply 37. doi: 10.1126/science.1202472.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden. anders.liljas@biochemistry.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719661" target="_blank"〉PubMed〈/a〉
Keywords:
GTP Phosphohydrolases/chemistry/metabolism
;
Guanosine Triphosphate/*analogs & derivatives/chemistry/*metabolism
;
Histidine/chemistry/metabolism
;
Hydrogen Bonding
;
Hydrolysis
;
Hydrophobic and Hydrophilic Interactions
;
Models, Molecular
;
Peptide Elongation Factor Tu/*chemistry/*metabolism
;
Phosphates/chemistry/metabolism
;
Protons
;
RNA, Bacterial/chemistry/metabolism
;
RNA, Ribosomal, 23S/chemistry/metabolism
;
RNA, Transfer, Amino Acyl/metabolism
;
Ribosomes/*metabolism
;
Water/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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