7BNY
Structure of 2A protein from encephalomyocarditis virus (EMCV)
Summary for 7BNY
| Entry DOI | 10.2210/pdb7bny/pdb |
| Descriptor | Genome polyprotein, SULFATE ION (3 entities in total) |
| Functional Keywords | emcv, cardiovirus, 2a, picornavirus, frameshifting, prf, rna-binding protein, protein-mediated frameshifting, ribosome-binding protein, beta-shell, viral protein |
| Biological source | Mengo encephalomyocarditis virus |
| Total number of polymer chains | 4 |
| Total formula weight | 72189.29 |
| Authors | Hill, C.H.,Napthine, S.,Pekarek, L.,Kibe, A.,Firth, A.E.,Graham, S.C.,Caliskan, N.,Brierley, I. (deposition date: 2021-01-22, release date: 2021-12-08, Last modification date: 2022-02-02) |
| Primary citation | Hill, C.H.,Pekarek, L.,Napthine, S.,Kibe, A.,Firth, A.E.,Graham, S.C.,Caliskan, N.,Brierley, I. Structural and molecular basis for Cardiovirus 2A protein as a viral gene expression switch. Nat Commun, 12:7166-7166, 2021 Cited by PubMed Abstract: Programmed -1 ribosomal frameshifting (PRF) in cardioviruses is activated by the 2A protein, a multi-functional virulence factor that also inhibits cap-dependent translational initiation. Here we present the X-ray crystal structure of 2A and show that it selectively binds to a pseudoknot-like conformation of the PRF stimulatory RNA element in the viral genome. Using optical tweezers, we demonstrate that 2A stabilises this RNA element, likely explaining the increase in PRF efficiency in the presence of 2A. Next, we demonstrate a strong interaction between 2A and the small ribosomal subunit and present a cryo-EM structure of 2A bound to initiated 70S ribosomes. Multiple copies of 2A bind to the 16S rRNA where they may compete for binding with initiation and elongation factors. Together, these results define the structural basis for RNA recognition by 2A, show how 2A-mediated stabilisation of an RNA pseudoknot promotes PRF, and reveal how 2A accumulation may shut down translation during virus infection. PubMed: 34887415DOI: 10.1038/s41467-021-27400-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.62 Å) |
Structure validation
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