2bv3

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Gudkov, A.T.]]
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[[Category: Gudkov, A T.]]
[[Category: Hansson, S.]]
[[Category: Hansson, S.]]
[[Category: Liljas, A.]]
[[Category: Liljas, A.]]
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[[Category: Logan, D.T.]]
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[[Category: Logan, D T.]]
[[Category: Singh, R.]]
[[Category: Singh, R.]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: translation mutation thr84ala]]
[[Category: translation mutation thr84ala]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:59 2008''

Revision as of 14:42, 21 February 2008


2bv3, resolution 2.50Å

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CRYSTAL STRUCTURE OF A MUTANT ELONGATION FACTOR G TRAPPED WITH A GTP ANALOGUE

Overview

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.

About this Structure

2BV3 is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure of a mutant elongation factor G trapped with a GTP analogue., Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT, FEBS Lett. 2005 Aug 15;579(20):4492-7. PMID:16083884

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