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3M94

Complex crystal structure of Ascaris suum eIF4E-3 with m2,2,7G cap

Summary for 3M94
Entry DOI10.2210/pdb3m94/pdb
Related3M93
DescriptorTranslation initiation factor 4E, Eukaryotic translation initiation factor 4E-binding protein 1, N,N,7-trimethylguanosine 5'-(trihydrogen diphosphate), ... (5 entities in total)
Functional Keywordseif4e, berkeley structural genomics center, bsgc, translation
Biological sourceAscaris suum (Pig roundworm)
More
Total number of polymer chains2
Total formula weight24845.24
Authors
Liu, W.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2010-03-19, release date: 2011-07-20, Last modification date: 2023-09-06)
Primary citationLiu, W.,Jankowska-Anyszka, M.,Piecyk, K.,Dickson, L.,Wallace, A.,Niedzwiecka, A.,Stepinski, J.,Stolarski, R.,Darzynkiewicz, E.,Kieft, J.,Zhao, R.,Jones, D.N.,Davis, R.E.
Structural basis for nematode eIF4E binding an m2,2,7G-Cap and its implications for translation initiation.
Nucleic Acids Res., 39:8820-8832, 2011
Cited by
PubMed Abstract: Metazoan spliced leader (SL) trans-splicing generates mRNAs with an m(2,2,7)G-cap and a common downstream SL RNA sequence. The mechanism for eIF4E binding an m²²⁷G-cap is unknown. Here, we describe the first structure of an eIF4E with an m(2,2,7)G-cap and compare it to the cognate m⁷G-eIF4E complex. These structures and Nuclear Magnetic Resonance (NMR) data indicate that the nematode Ascaris suum eIF4E binds the two different caps in a similar manner except for the loss of a single hydrogen bond on binding the m(2,2,7)G-cap. Nematode and mammalian eIF4E both have a low affinity for m(2,2,7)G-cap compared with the m⁷G-cap. Nematode eIF4E binding to the m⁷G-cap, m(2,2,7)G-cap and the m(2,2,7)G-SL 22-nt RNA leads to distinct eIF4E conformational changes. Additional interactions occur between Ascaris eIF4E and the SL on binding the m(2,2,7)G-SL. We propose interactions between Ascaris eIF4E and the SL impact eIF4G and contribute to translation initiation, whereas these interactions do not occur when only the m(2,2,7)G-cap is present. These data have implications for the contribution of 5'-UTRs in mRNA translation and the function of different eIF4E isoforms.
PubMed: 21965542
DOI: 10.1093/nar/gkr650
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

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