%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture non répertoriées par l'AERES
%A Qu, C.
%A Liljas, L.
%A Opalka, N.
%A Brugidou, Christophe
%A Yeager, M.
%A Beachy, R.N.
%A Fauquet, Claude
%A Johnson, J.E
%A Lin, T.
%T 3D domain swapping modulates the stability of members of an icosahedral virus group
%D 2000
%L fdi:010024715
%G ENG
%J Structure
%K PHYTOVIRUS ; RIZ ; ANALYSE STRUCTURALE ; CRISTALLOGRAPHIE ; PROTEINE ; CAPSIDE ; STRUCTURE SPATIALE ; SUBSTANCE CRISTALLISEE ; PROPRIETE PHYSIQUE ; STABILITE STRUCTURALE ; GENOME
%K STRUCTURE 3D ; SYMETRIE ICOSAHEDRALE
%P 1095-1103
%R 10.1016/S0969-2126(00)00508-6
%U https://www.documentation.ird.fr/hor/fdi:010024715
%> https://horizon.documentation.ird.fr/exl-doc/pleins_textes/pleins_textes_7/b_fdi_57-58/010024715.pdf
%V 8
%W Horizon (IRD)
%X Background : Rice yellow mottle virus (RYMV) is a major pathogen that dramatically reduces rice production in many African countries. RYMV belongs to the genus sobemovirus, one group of plant viruses with icosahedral capsids and single-stranded, positive-sense RNA genomes. Results: The structure of RYMV was determined and refined to 2.8 A resolution by X-ray crystallography. The capsid contains 180 copies of the coat protein subunit arranged with T = 3 icosahedral symmetry. Each subunit adopts a jelly-roll Beta sandwich fold. The RYMV capsid structure is similar to those of other sobemoviruses. When compared with these viruses, however, the BetaA arm of the RYMV subunit, which is a molecular switch that regulates quasi-equivalent subunit interactions, is swapped with the 2-fold-related BetaA arm to a similar, noncovalent bonding environment. This exchange of identical structural elements across a symmetry axis is categorized as 3D domain swapping and produces long-range interactions throughout the icosahedral surface lattice. Biochemical analysis supports the notion that 3D domain swapping increases the stability of RYMV. (Résumé d'auteur)
%$ 076MALPLA