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Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
2015 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 5, 15817Article in journal (Refereed) Published
Abstract [en]

Protein synthesis on the ribosome involves hydrolysis of GTP in several key steps of the mRNA translation cycle. These steps are catalyzed by the translational GTPases of which elongation factor Tu (EF-Tu) is the fastest GTPase known. Here, we use extensive computer simulations to explore the origin of its remarkably high catalytic rate on the ribosome and show that it is made possible by a very large positive activation entropy. This entropy term (T Delta S-double dagger) amounts to more than 7 kcal/mol at 25 degrees C. It is further found to be characteristic of the reaction mechanism utilized by the translational, but not other, GTPases and it enables these enzymes to attain hydrolysis rates exceeding 500 s(-1). This entropy driven mechanism likely reflects the very high selection pressure on the speed of protein synthesis, which drives the rate of each individual GTPase towards maximal turnover rate of the whole translation cycle.

Place, publisher, year, edition, pages
2015. Vol. 5, 15817
National Category
Cell and Molecular Biology
URN: urn:nbn:se:uu:diva-267197DOI: 10.1038/srep15817ISI: 000363412700001PubMedID: 26497916OAI: oai:DiVA.org:uu-267197DiVA: diva2:872537
Knut and Alice Wallenberg FoundationSwedish Research CouncilSwedish National Infrastructure for Computing (SNIC), 25/2-10
Available from: 2015-11-19 Created: 2015-11-19 Last updated: 2016-04-08Bibliographically approved

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