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Crystal Structure of Potato Leafroll Virus (PLRV) Coat Protein
Structural highlights
FunctionCAPSD_PLRV1 Major capsid protein that self-assembles to form an icosahedral capsid with a T=3 symmetry, about 23 nm in diameter, and consisting of 180 capsid proteins monomers (PubMed:31611039, PubMed:34813955). Most of the 180 monomers are the major capsid protein, but a small percentage contain the minor capsid protein, which has a long C-terminal extension (PubMed:31611039).[1] [2] Publication Abstract from PubMedLuteoviruses, 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-A 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. Crystal structure of the potato leafroll virus coat protein and implications for viral assembly.,Adams MC, Schiltz CJ, Heck ML, Chappie JS J Struct Biol. 2021 Nov 20;214(1):107811. doi: 10.1016/j.jsb.2021.107811. PMID:34813955[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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