7RLM
Crystal Structure of Potato Leafroll Virus (PLRV) Coat Protein
Summary for 7RLM
| Entry DOI | 10.2210/pdb7rlm/pdb |
| Descriptor | Coat protein, BROMIDE ION (3 entities in total) |
| Functional Keywords | plrv, polerovirus, icosahedral virus, quasi-equivalence, viral assembly, capsid, plant virus, viral protein |
| Biological source | Potato leafroll virus (PLrV) |
| Total number of polymer chains | 6 |
| Total formula weight | 93496.39 |
| Authors | Adams, M.C.,Chappie, J.S.,Schiltz, C.J. (deposition date: 2021-07-25, release date: 2022-01-19, Last modification date: 2023-10-18) |
| Primary citation | Adams, M.C.,Schiltz, C.J.,Heck, M.L.,Chappie, J.S. Crystal structure of the potato leafroll virus coat protein and implications for viral assembly. J.Struct.Biol., 214:107811-107811, 2021 Cited by PubMed Abstract: Luteoviruses, poleroviruses, and enamoviruses are insect-transmitted, agricultural pathogens that infect a wide array of plants, including staple food crops. Previous cryo-electron microscopy studies of virus-like particles show that luteovirid viral capsids are built from a structural coat protein that organizes with T = 3 icosahedral symmetry. Here, we present the crystal structure of a truncated version of the coat protein monomer from potato leafroll virus at 1.80-Å resolution. In the crystal lattice, monomers pack into flat sheets that preserve the two-fold and three-fold axes of icosahedral symmetry and show minimal structural deviations when compared to the full-length subunits of the assembled virus-like particle. These observations have important implications in viral assembly and maturation and suggest that the CP N-terminus and its interactions with RNA play an important role in generating capsid curvature. PubMed: 34813955DOI: 10.1016/j.jsb.2021.107811 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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