Crystal structure of a mutant elongation factor G trapped with a GTP analogue
Hansson, Sebastian LU ; Singh, Ranvir LU ; Gudkov, A T ; Liljas, Anders LU and Logan, Derek LU
(2005)
In FEBS Letters
579(20).
p.4492-4497
- Abstract
- Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. (c) 2005 Federation of European Biochemical Societies.... (More)
- Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/152245
- author
- Hansson, Sebastian
LU
; Singh, Ranvir
LU
; Gudkov, A T
; Liljas, Anders
LU
and Logan, Derek
LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- FEBS Letters
- volume
- 579
- issue
- 20
- pages
- 4492 - 4497
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000231350900048
- pmid:16083884
- scopus:23644451172
- ISSN
- 1873-3468
- DOI
- 10.1016/j.febslet.2005.07.016
- language
- English
- LU publication?
- yes
- id
- 17f9b9f9-a1d5-41c3-9f48-0c51db89e74c (old id 152245)
- date added to LUP
- 2016-04-01 15:38:45
- date last changed
- 2022-02-12 08:59:51
@article{17f9b9f9-a1d5-41c3-9f48-0c51db89e74c,
abstract = {{Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.}},
author = {{Hansson, Sebastian and Singh, Ranvir and Gudkov, A T and Liljas, Anders and Logan, Derek}},
issn = {{1873-3468}},
language = {{eng}},
number = {{20}},
pages = {{4492--4497}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{Crystal structure of a mutant elongation factor G trapped with a GTP analogue}},
url = {{http://dx.doi.org/10.1016/j.febslet.2005.07.016}},
doi = {{10.1016/j.febslet.2005.07.016}},
volume = {{579}},
year = {{2005}},
}