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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)
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author
organization
publishing date
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
2007-07-09 15:24:08
date last changed
2017-11-19 04:05:04
@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},
  volume       = {579},
  year         = {2005},
}