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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Modeling the mechanisms of biological GTP hydrolysis

Author

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

Summary, in English

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.

Publishing year

2015-09-15

Language

English

Pages

80-90

Publication/Series

Archives of Biochemistry and Biophysics

Volume

582

Document type

Journal article review

Publisher

Academic Press

Keywords

  • Computational Biology
  • Guanosine Triphosphate/metabolism
  • Hydrolysis
  • Models, Biological
  • Peptide Elongation Factor Tu/metabolism
  • ras Proteins/metabolism

Status

Published

ISBN/ISSN/Other

  • ISSN: 0003-9861