Modeling the mechanisms of biological GTP hydrolysis
Carvalho, Alexandra T P ; Szeler, Klaudia ; Vavitsas, Konstantinos ; Åqvist, Johan and Kamerlin, Shina C L LU
(2015)
In Archives of Biochemistry and Biophysics
582.
p.80-90
- 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... (More)
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.
(Less)
- author
- Carvalho, Alexandra T P
; Szeler, Klaudia
; Vavitsas, Konstantinos
; Åqvist, Johan
and Kamerlin, Shina C L
LU
- publishing date
- 2015-09-15
- type
- Contribution to journal
- publication status
- published
- keywords
- Computational Biology, Guanosine Triphosphate/metabolism, Hydrolysis, Models, Biological, Peptide Elongation Factor Tu/metabolism, ras Proteins/metabolism
- in
- Archives of Biochemistry and Biophysics
- volume
- 582
- pages
- 11 pages
- publisher
- Academic Press
- external identifiers
-
- pmid:25731854
- scopus:84940718637
- ISSN
- 0003-9861
- DOI
- 10.1016/j.abb.2015.02.027
- language
- English
- LU publication?
- no
- additional info
- Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.
- id
- fcd7416a-eba3-4671-b28d-795b999162e1
- date added to LUP
- 2025-01-11 21:38:30
- date last changed
- 2025-03-23 10:23:21
@article{fcd7416a-eba3-4671-b28d-795b999162e1,
abstract = {{<p>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.</p>}},
author = {{Carvalho, Alexandra T P and Szeler, Klaudia and Vavitsas, Konstantinos and Åqvist, Johan and Kamerlin, Shina C L}},
issn = {{0003-9861}},
keywords = {{Computational Biology; Guanosine Triphosphate/metabolism; Hydrolysis; Models, Biological; Peptide Elongation Factor Tu/metabolism; ras Proteins/metabolism}},
language = {{eng}},
month = {{09}},
pages = {{80--90}},
publisher = {{Academic Press}},
series = {{Archives of Biochemistry and Biophysics}},
title = {{Modeling the mechanisms of biological GTP hydrolysis}},
url = {{http://dx.doi.org/10.1016/j.abb.2015.02.027}},
doi = {{10.1016/j.abb.2015.02.027}},
volume = {{582}},
year = {{2015}},
}