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Science. 2011 Jul 1;333(6038):37; author reply 37. doi: 10.1126/science.1202472.

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

Author information

1
Department of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden. anders.liljas@biochemistry.lu.se

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.

PMID:
21719661
DOI:
10.1126/science.1202472
[Indexed for MEDLINE]
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