5ME5

Crystal Structure of eiF4E from C. melo bound to a eIF4G peptide

Summary for 5ME5

• Entry DOI: 10.2210/pdb5me5/pdb
• Descriptor: Eukaryotic transcription initiation factor 4E, eIF4G, SULFATE ION, ... (4 entities in total)
• Functional Keywords: translation initiation eif4f complex, translation
• Biological source: Cucumis melo (Muskmelon); More
• Total number of polymer chains: 2
• Total formula weight: 36727.14

Authors

Querol-Audi, J.,Silva, C.,Miras, M.,Truniger, V.,Aranda-Regules, M.,Verdaguer, N. (deposition date: 2016-11-14, release date: 2017-08-23)

Primary citation

Miras, M.,Truniger, V.,Silva, C.,Verdaguer, N.,Aranda, M.A.,Querol-Audi, J.
Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation.
Plant Physiol., 174:1476-1491, 2017

PubMed Abstract: The association-dissociation of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation. The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a single canonical alpha-helical motif, while metazoan eIF4E-binding proteins (m4E-BPs) advantageously compete against eIF4G via bimodal interactions involving this canonical motif and a second noncanonical motif of the eIF4E surface. Metazoan eIF4Gs share this extended binding interface with m4E-BPs, with significant implications on the understanding of translation regulation and the design of therapeutic molecules. Here we show the high-resolution structure of melon () eIF4E in complex with a melon eIF4G peptide and propose the first eIF4E-eIF4G structural model for plants. Our structural data together with functional analyses demonstrate that plant eIF4G binds to eIF4E through both the canonical and noncanonical motifs, similarly to metazoan eIF4E-eIF4G complexes. As in the case of metazoan eIF4E-eIF4G, this may have very important practical implications, as plant eIF4E-eIF4G is also involved in a significant number of plant diseases. In light of our results, a universal eukaryotic bipartite mode of binding to eIF4E is proposed.

PubMed: 28522457
DOI: 10.1104/pp.17.00193

Experimental method

X-RAY DIFFRACTION (1.9 Å)