6OZU

Crystal structure of the MIF4G domain of Trypanosoma cruzi translation initiation factor EIF4G5

Summary for 6OZU

• Entry DOI: 10.2210/pdb6ozu/pdb
• Descriptor: Eukaryotic translation initiation factor 4 gamma 5, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: initiation factor, eif4g, translation
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 2
• Total formula weight: 58298.52

Authors

Guimaraes, B.G.,Santos, L.P.C. (deposition date: 2019-05-16, release date: 2019-12-11, Last modification date: 2024-05-15)

Primary citation

Camillo Dos Santos, L.P.,de Matos, B.M.,de Maman Ribeiro, B.C.,Zanchin, N.I.T.,Guimaraes, B.G.
Crystal structure of the MIF4G domain of the Trypanosoma cruzi translation initiation factor EIF4G5.
Acta Crystallogr.,Sect.F, 75:738-743, 2019

PubMed Abstract: Kinetoplastida, a class of early-diverging eukaryotes that includes pathogenic Trypanosoma and Leishmania species, display key differences in their translation machinery compared with multicellular eukaryotes. One of these differences involves a larger number of genes encoding eIF4E and eIF4G homologs and the interaction pattern between the translation initiation factors. eIF4G is a scaffold protein which interacts with the mRNA cap-binding factor eIF4E, the poly(A)-binding protein, the RNA helicase eIF4A and the eIF3 complex. It contains the so-called middle domain of eIF4G (MIF4G), a multipurpose adaptor involved in different protein-protein and protein-RNA complexes. Here, the crystal structure of the MIF4G domain of T. cruzi EIF4G5 is described at 2.4 Å resolution, which is the first three-dimensional structure of a trypanosomatid MIF4G domain to be reported. Structural comparison with IF4G homologs from other eukaryotes and other MIF4G-containing proteins reveals differences that may account for the specific interaction mechanisms of MIF4G despite its highly conserved overall fold.

PubMed: 31797815
DOI: 10.1107/S2053230X19015061

Experimental method

X-RAY DIFFRACTION (2.4 Å)