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DP02399 - Eukaryotic translation initiation factor 4E

Organism Homo sapiens

Gene EIF4E (EIF4EL1, EIF4F)

Sequence length 217

Disorder content 16.1%

Cross references UniProtKB:P06730, MobiDB:P06730

Dataset(s) NDDs-related proteinsRNA-binding proteins

Last update 2022-02-14

Entry history

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DP02399r004 Structural state

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Term disorder, IDPO:00076

Fragment 1 - 26

Evidence X-ray crystallography-based structural model with missing residue coordinates used in manual assertion, ECO:0006220

Cross references PDB:1IPB PDB:1IPC

Reference Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region. Tomoo K, Shen X, Okabe K, Nozoe Y, Fukuhara S, Morino S, Ishida T, Taniguchi T, Hasegawa H, Terashima A, Sasaki M, Katsuya Y, Kitamura K, Miyoshi H, Ishikawa M, Miura K. Biochem J, 2002, pmid:11879179

Statements Abstract "The present results provide the structural basis for the biological function of both N- and C-terminal mobile regions of eIF4E in translation initiation, especially the regulatory function through the switch-on/off of eIF4E-binding protein–eIF4E phosphorylation." Introduction "However, the structures of the N- and C-terminal regions are still unclear, because of the high flexibility of these regions in eIF4E." Results "As is shown in Figure 1, we could determine the structure from Glu27 (in both complexes of human full-length eIF4E; it was impossible to determine the structure from the N-terminus to Gln26 because of the high flexibility." Figure "In contrast with large flexibility at both N- and C-terminal regions, the core regions consisting of eight-stranded anti-parallel b-sheets and three long a-helices are very similar to each other."

Curator Veronika Ács

validated by Edoardo Salladini

DP02399r003 Structural state

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Term disorder, IDPO:00076

Fragment 2 - 35

Evidence nuclear magnetic resonance spectroscopy evidence used in manual assertion, ECO:0006165

Cross references PDB:2GPQ

Reference Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands. Volpon L, Osborne MJ, Topisirovic I, Siddiqui N, Borden KL. EMBO J, 2006, pmid:17036047

Statements Results "In this NMR ensemble of the apo-eIF4E, the loops S1–S2, H2–S3, H4–S5 and S7–S8 are less defined while the first 35 residues at the N-terminus are completely disordered." Curator statement "The authors mention in the Results and discussion section that the N-terminal methionine is removed from the protein: As can be seen in Figure 2A, the molecular mass of eIF4E is 24964.373.2 Da slightly less than the predicted mass 25097.2 Da. This mass difference (132.9 Da) corresponds to the loss of methionine (131.2 Da) at the N-terminus, which is a common event (Huang et al, 1987). The absence of Met1 in the NMR data corroborates this hypothesis."

Curator Veronika Ács

validated by Edoardo Salladini

DP02399r001 Structural state

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Term disorder, IDPO:00076

Fragment 1 - 29

Evidence X-ray crystallography-based structural model with missing residue coordinates used in manual assertion, ECO:0006220

Cross references PDB:5T46

Reference The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. Grüner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E. Mol Cell, 2016, pmid:27773676

Statements Results "The N-terminal Regions of Hs and Dm eIF4E Are Not Required for Binding to eIF4G" Results "Although full-length eIF4E was used in the human complex, the first 29 residues (M1–A29) are not visible in the electron density map"

Curator Federica Quaglia

validated by Edoardo Salladini

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DP02399 - Eukaryotic translation initiation factor 4E