2LGT
Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F
Summary for 2LGT
| Entry DOI | 10.2210/pdb2lgt/pdb |
| NMR Information | BMRB: 17822 |
| Descriptor | Eukaryotic peptide chain release factor subunit 1 (1 entity in total) |
| Functional Keywords | translation |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P62495 |
| Total number of polymer chains | 1 |
| Total formula weight | 16079.64 |
| Authors | Wong, L.E.,Li, Y.,Pillay, S.,Pervushin, K. (deposition date: 2011-08-02, release date: 2012-03-14, Last modification date: 2024-05-01) |
| Primary citation | Wong, L.E.,Li, Y.,Pillay, S.,Frolova, L.,Pervushin, K. Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1 Nucleic Acids Res., 2012 Cited by PubMed Abstract: Translation termination in eukaryotes is catalyzed by two release factors eRF1 and eRF3 in a cooperative manner. The precise mechanism of stop codon discrimination by eRF1 remains obscure, hindering drug development targeting aberrations at translation termination. By solving the solution structures of the wild-type N-domain of human eRF1 exhibited omnipotent specificity, i.e. recognition of all three stop codons, and its unipotent mutant with UGA-only specificity, we found the conserved GTS loop adopting alternate conformations. We propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. To explore such feasibility, we positioned N-domain in a pre-termination ribosomal complex using the binding interface between N-domain and model RNA oligonucleotides mimicking Helix 44 of 18S rRNA. NMR analysis revealed that those duplex RNA containing 2-nt internal loops interact specifically with helix α1 of N-domain, and displace C-domain from a non-covalent complex of N-domain and C-domain, suggesting domain rearrangement in eRF1 that accompanies N-domain accommodation into the ribosomal A site. PubMed: 22383581DOI: 10.1093/nar/gks192 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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