EF-Tu and EF-G are activated by allosteric effects.
Proc Natl Acad Sci U S A
; 115(13): 3386-3391, 2018 03 27.
Article
em En
| MEDLINE
| ID: mdl-29531062
ABSTRACT
Many cellular processes are controlled by GTPases, and gaining quantitative understanding of the activation of such processes has been a major challenge. In particular, it is crucial to obtain reliable free-energy surfaces for the relevant reaction paths both in solution and in GTPases active sites. Here, we revisit the energetics of the activation of EF-G and EF-Tu by the ribosome and explore the nature of the catalysis of the GTPase reaction. The comparison of EF-Tu to EF-G allows us to explore the impact of possible problems with the available structure of EF-Tu. Additionally, mutational effects are used for a careful validation of the emerging conclusions. It is found that the reaction may proceed by both a two-water mechanism and a one-water (GTP as a base) mechanism. However, in both cases, the activation involves a structural allosteric effect, which is likely to be a general-activation mechanism for all GTPases.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fator Tu de Elongação de Peptídeos
/
Fator G para Elongação de Peptídeos
/
Guanosina Trifosfato
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article