Qu C., Liljas L., Opalka N., Brugidou Christophe, Yeager M., Beachy R.N., Fauquet Claude, Johnson J.E, Lin T. (2000). 3D domain swapping modulates the stability of members of an icosahedral virus group. Structure, 8, p. 1095-1103.
Titre du document
3D domain swapping modulates the stability of members of an icosahedral virus group
Année de publication
2000
Type de document
Article
Auteurs
Qu C., Liljas L., Opalka N., Brugidou Christophe, Yeager M., Beachy R.N., Fauquet Claude, Johnson J.E, Lin T.
Source
Structure, 2000,
8, p. 1095-1103
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)
