Modeling the mechanisms of biological GTP hydrolysis.

Carvalho AT, Szeler K, Vavitsas K, Åqvist J, Kamerlin SC

Arch. Biochem. Biophys. 582 (-) 80-90 [2015-09-15; online 2015-02-27]

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.

Affiliated researcher

PubMed 25731854

DOI 10.1016/j.abb.2015.02.027

Crossref 10.1016/j.abb.2015.02.027

pii: S0003-9861(15)00089-2


Publications 7.1.2