1EFU
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI
1EFU の概要
| エントリーDOI | 10.2210/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: 8596629DOI: 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) |
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