2V6C

Crystal structure of ErbB3 binding protein 1 (Ebp1)

2V6C の概要

• エントリーDOI: 10.2210/pdb2v6c/pdb
• 分子名称: PROLIFERATION-ASSOCIATED PROTEIN 2G4 (2 entities in total)
• 機能のキーワード: translation regulation, translational regulator, rna-binding, acetylation, rna binding, transcription, cobalt, nucleus, repressor, hydrolase, cytoplasm, transcription regulator, transcription regulation, phosphorylation, rrna processing, ribonucleoprotein
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39387.07

構造登録者

Monie, T.P.,Perrin, A.J.,Birtley, J.R.,Curry, S. (登録日: 2007-07-16, 公開日: 2007-08-21, 最終更新日: 2023-12-13)

主引用文献

Monie, T.P.,Perrin, A.J.,Birtley, J.R.,Sweeney, T.R.,Karakasiliotis, I.,Chaudry, Y.,Roberts, L.O.,Matthews, S.,Goodfellow, I.G.,Curry, S.
Structural Insights Into the Transcriptional and Translational Roles of Ebp1
Embo J., 26:3936-, 2007

PubMed Abstract: The ErbB3-binding protein 1 (Ebp1) is an important regulator of transcription, affecting eukaryotic cell growth, proliferation, differentiation and survival. Ebp1 can also affect translation and cooperates with the polypyrimidine tract-binding protein (PTB) to stimulate the activity of the internal ribosome entry site (IRES) of foot-and-mouth disease virus (FMDV). We report here the crystal structure of murine Ebp1 (p48 isoform), providing the first glimpse of the architecture of this versatile regulator. The structure reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal extension that contains important motifs for binding proteins and RNA. It sheds new light on the conformational differences between the p42 and p48 isoforms of Ebp1, the disposition of the key protein-interacting motif ((354)LKALL(358)) and the RNA-binding activity of Ebp1. We show that the primary RNA-binding site is formed by a Lys-rich motif in the C terminus and mediates the interaction with the FMDV IRES. We also demonstrate a specific functional requirement for Ebp1 in FMDV IRES-directed translation that is independent of a direct interaction with PTB.

PubMed: 17690690
DOI: 10.1038/SJ.EMBOJ.7601817

実験手法

X-RAY DIFFRACTION (2.5 Å)