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1EFU

ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

1EFU の概要
エントリーDOI10.2210/pdb1efu/pdb
分子名称ELONGATION FACTOR TU, ELONGATION FACTOR TS (3 entities in total)
機能のキーワードelongation factor, complex (two elongation factors)
由来する生物種Escherichia coli
詳細
タンパク質・核酸の鎖数4
化学式量合計145125.93
構造登録者
Kawashima, T.,Berthet-Colominas, C.,Wulff, M.,Cusack, S.,Leberman, R. (登録日: 1996-07-09, 公開日: 1997-01-11, 最終更新日: 2024-02-07)
主引用文献Kawashima, T.,Berthet-Colominas, C.,Wulff, M.,Cusack, S.,Leberman, R.
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.
Nature, 379:511-518, 1996
Cited by
PubMed Abstract: The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.
PubMed: 8596629
DOI: 10.1038/379511a0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1efu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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