2BV3

Crystal structure of a mutant elongation factor G trapped with a GTP analogue

2BV3 の概要

• エントリーDOI: 10.2210/pdb2bv3/pdb
• 関連するPDBエントリー: 1DAR 1EFG 1ELO 1FNM 1IP8 1IPM 1IPO 1IPR 1JQM 1JQS 1KTV 1PN6 2BM0 2BM1 2EFG
• 分子名称: ELONGATION FACTOR G, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: switch ii, elongation factor, gtp-binding, translation mutation thr84ala, protein biosynthesis
• 由来する生物種: THERMUS THERMOPHILUS
• 細胞内の位置: Cytoplasm: P13551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77303.34

構造登録者

Hansson, S.,Singh, R.,Gudkov, A.T.,Liljas, A.,Logan, D.T. (登録日: 2005-06-22, 公開日: 2005-08-10, 最終更新日: 2023-12-13)

主引用文献

Hansson, S.,Singh, R.,Gudkov, A.T.,Liljas, A.,Logan, D.T.
Crystal Structure of a Mutant Elongation Factor G Trapped with a GTP Analogue.
FEBS Lett., 579:4492-, 2005

PubMed 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.

PubMed: 16083884
DOI: 10.1016/J.FEBSLET.2005.07.016

実験手法

X-RAY DIFFRACTION (2.5 Å)