2V6C
Crystal structure of ErbB3 binding protein 1 (Ebp1)
Summary for 2V6C
| Entry DOI | 10.2210/pdb2v6c/pdb |
| Descriptor | PROLIFERATION-ASSOCIATED PROTEIN 2G4 (2 entities in total) |
| Functional Keywords | translation regulation, translational regulator, rna-binding, acetylation, rna binding, transcription, cobalt, nucleus, repressor, hydrolase, cytoplasm, transcription regulator, transcription regulation, phosphorylation, rrna processing, ribonucleoprotein |
| Biological source | MUS MUSCULUS (MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 39387.07 |
| Authors | Monie, T.P.,Perrin, A.J.,Birtley, J.R.,Curry, S. (deposition date: 2007-07-16, release date: 2007-08-21, Last modification date: 2023-12-13) |
| Primary citation | 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 Cited by 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: 17690690DOI: 10.1038/SJ.EMBOJ.7601817 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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