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Comment on "The mechanism for activation of GTP hydrolysis on the ribosome"
Department of Biochemistry and Structural Biology, Lund University.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational and Systems Biology.
2011 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 333, no 6038, 37- p.Article in journal (Refereed) Published
Abstract [en]

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.
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Structural Biology
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URN: urn:nbn:se:uu:diva-170002DOI: 10.1126/science.1202472OAI: oai:DiVA.org:uu-170002DiVA: diva2:508158
Available from: 2012-03-07 Created: 2012-03-07 Last updated: 2017-12-07Bibliographically approved

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