Modeling the mechanisms of biological GTP hydrolysis

Alexandra T.P. Carvalho, Klaudia Szeler, Konstantinos Vavitsas, Johan Åqvist, Shina C.L. Kamerlin

31 Citations (Scopus)

Abstract

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 γ-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.

Original languageEnglish
JournalArchives of Biochemistry and Biophysics
Volume582
Pages (from-to)80-90
Number of pages11
ISSN0003-9861
DOIs
Publication statusPublished - 15 Sept 2015

Fingerprint

Dive into the research topics of 'Modeling the mechanisms of biological GTP hydrolysis'. Together they form a unique fingerprint.

Cite this