Modeling the mechanisms of biological GTP hydrolysis
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
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.
GTP hydrolysis, Ras GTPase, EF-Tu, EF-G, Computational biology
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-264885DOI: 10.1016/j.abb.2015.02.027ISI: 000360781200009PubMedID: 25731854OAI: oai:DiVA.org:uu-264885DiVA: diva2:861931
FunderSwedish Research CouncilKnut and Alice Wallenberg Foundation