Modeling the mechanisms of biological GTP hydrolysis

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

doi:10.1016/j.abb.2015.02.027

Modeling the mechanisms of biological GTP hydrolysis

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

Molekylær Plantebiologi

31 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Archives of Biochemistry and Biophysics
Vol/bind	582
Sider (fra-til)	80-90
Antal sider	11
ISSN	0003-9861
DOI	https://doi.org/10.1016/j.abb.2015.02.027
Status	Udgivet - 15 sep. 2015

Emneord

Computational biology
EF-G
EF-Tu
GTP hydrolysis
Ras GTPase

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10.1016/j.abb.2015.02.027Licens: CC BY-NC-ND

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title = "Modeling the mechanisms of biological GTP hydrolysis",

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.",

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AU - Carvalho, Alexandra T.P.

AU - Szeler, Klaudia

AU - Vavitsas, Konstantinos

AU - Åqvist, Johan

AU - Kamerlin, Shina C.L.

N1 - Special issue in computational modeling on biological systems

PY - 2015/9/15

Y1 - 2015/9/15

N2 - 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.

AB - 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.

KW - Computational biology

KW - EF-G

KW - EF-Tu

KW - GTP hydrolysis

KW - Ras GTPase

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DO - 10.1016/j.abb.2015.02.027

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SP - 80

EP - 90

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

Modeling the mechanisms of biological GTP hydrolysis

Abstract

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