5W2F
Crystal Structure of the C-terminal Domain of Human eIF2D at 1.4 A resolution
Summary for 5W2F
| Entry DOI | 10.2210/pdb5w2f/pdb |
| Descriptor | Eukaryotic translation initiation factor 2D, FORMIC ACID (3 entities in total) |
| Functional Keywords | re-initiation, ribosome, eif2, translation |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23199.92 |
| Authors | Vaidya, A.T.,Lomakin, I.B.,Joseph, N.N.,Dmitriev, S.E.,Steitz, T.A. (deposition date: 2017-06-06, release date: 2017-08-02, Last modification date: 2024-03-13) |
| Primary citation | Vaidya, A.T.,Lomakin, I.B.,Joseph, N.N.,Dmitriev, S.E.,Steitz, T.A. Crystal Structure of the C-terminal Domain of Human eIF2D and Its Implications on Eukaryotic Translation Initiation. J. Mol. Biol., 429:2765-2771, 2017 Cited by PubMed Abstract: Protein synthesis is a key process in all living organisms. In eukaryotes, initiation factor 2 (eIF2) plays an important role in translation initiation as it selects and delivers the initiator tRNA to the small ribosomal subunit. Under stress conditions, phosphorylation of the α-subunit of eIF2 downregulates cellular protein synthesis. However, translation of certain mRNAs continues via the eIF2D-dependent non-canonical initiation pathway. The molecular mechanism of this process remains elusive. In addition, eIF2D plays a role in translation re-initiation and ribosome recycling. Currently, there has been no structural information of eIF2D. We have now determined the crystal structure of the C-terminal domains of eIF2D at 1.4-Å resolution. One domain has the fold similar to that of eIF1, which is crucial for the scanning and initiation codon selection. The second domain has a known SWIB/MDM2 fold, which was not observed before in other translation initiation factors. Our structure reveals atomic details of inter-domain interactions in the C-terminal part of eIF2D and sheds light on the possible role of these domains in eIF2D during translation. PubMed: 28736176DOI: 10.1016/j.jmb.2017.07.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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