2IX8

MODEL FOR EEF3 BOUND TO AN 80S RIBOSOME

2IX8 の概要

• エントリーDOI: 10.2210/pdb2ix8/pdb
• EMDBエントリー: 1233
• 分子名称: ELONGATION FACTOR 3A (1 entity in total)
• 機能のキーワード: nucleotide-binding, protein biosynthesis, phosphorylation, elongation factor, rna-binding, atp-binding, rrna-binding
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cytoplasm : P16521
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 109441.55

構造登録者

Andersen, C.B.F.,Becker, T.,Blau, M.,Anand, M.,Halic, M.,Balar, B.,Mielke, T.,Boesen, T.,Pedersen, J.S.,Spahn, C.M.T.,Kinzy, T.G.,Andersen, G.R.,Beckmann, R. (登録日: 2006-07-07, 公開日: 2007-07-10, 最終更新日: 2024-10-16)

主引用文献

Andersen, C.B.F.,Becker, T.,Blau, M.,Anand, M.,Halic, M.,Balar, B.,Mielke, T.,Boesen, T.,Pedersen, J.S.,Spahn, C.M.T.,Kinzy, T.G.,Andersen, G.R.,Beckmann, R.
Structure of Eef3 and the Mechanism of Transfer RNA Release from the E-Site.
Nature, 443:663-668, 2006

PubMed Abstract: Elongation factor eEF3 is an ATPase that, in addition to the two canonical factors eEF1A and eEF2, serves an essential function in the translation cycle of fungi. eEF3 is required for the binding of the aminoacyl-tRNA-eEF1A-GTP ternary complex to the ribosomal A-site and has been suggested to facilitate the clearance of deacyl-tRNA from the E-site. Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains, with a chromodomain inserted in ABC2. Moreover, we present the cryo-electron microscopy structure of the ATP-bound form of eEF3 in complex with the post-translocational-state 80S ribosome from yeast. eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release.

PubMed: 16929303
DOI: 10.1038/nature05126

実験手法

ELECTRON MICROSCOPY (9.9 Å)