Comment on "The mechanism for activation of GTP hydrolysis on the ribosome"
2011 (English)In: Science, ISSN 0036-8075, Vol. 333, no 6038, 37- p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2011. Vol. 333, no 6038, 37- p.
IdentifiersURN: urn:nbn:se:uu:diva-170002DOI: 10.1126/science.1202472OAI: oai:DiVA.org:uu-170002DiVA: diva2:508158