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Modeling the mechanisms of biological GTP hydrolysis
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Univ Copenhagen, Dept Plant & Environm Sci, CPSC, DK-1871 Frederiksberg C, Denmark..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational and Systems Biology. Uppsala University, Science for Life Laboratory, SciLifeLab.
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2015 (English)In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 582, no SI, 80-90 p.Article, review/survey (Refereed) Published
Abstract [en]

Enzymes that hydrolyze GTP are currently in the spotlight, due to their molecular switch mechanism that controls many cellular processes. One of the best-known classes of these enzymes are small GTPases such as members of the Ras superfamily, which catalyze the hydrolysis of the gamma-phosphate bond in GTP. In addition, the availability of an increasing number of crystal structures of translational GTPases such as EF-Tu and EF-G have made it possible to probe the molecular details of GTP hydrolysis on the ribosome. However, despite a wealth of biochemical, structural and computational data, the way in which GTP hydrolysis is activated and regulated is still a controversial topic and well-designed simulations can play an important role in resolving and rationalizing the experimental data. In this review, we discuss the contributions of computational biology to our understanding of GTP hydrolysis on the ribosome and in small GTPases.

Place, publisher, year, edition, pages
2015. Vol. 582, no SI, 80-90 p.
Keyword [en]
GTP hydrolysis, Ras GTPase, EF-Tu, EF-G, Computational biology
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-264885DOI: 10.1016/j.abb.2015.02.027ISI: 000360781200009PubMedID: 25731854OAI: oai:DiVA.org:uu-264885DiVA: diva2:861931
Funder
Swedish Research CouncilKnut and Alice Wallenberg Foundation
Available from: 2015-10-19 Created: 2015-10-19 Last updated: 2017-12-01Bibliographically approved

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Szeler, KlaudiaÅqvist, JohanKamerlin, Lynn Shina C.

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