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 C 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. CONCLUSIONS: The quasi-equivalent interactions between the RYMV proteins are regulated by the N-terminal ordered residues of the betaA arm, which functions as a molecular switch. Comparative analysis suggests that this molecular switch can also modulate the stability of the viral capsids.
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 C 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. CONCLUSIONS: The quasi-equivalent interactions between the RYMV proteins are regulated by the N-terminal ordered residues of the betaA arm, which functions as a molecular switch. Comparative analysis suggests that this molecular switch can also modulate the stability of the viral capsids.
Authors: Dmitri Ivanov; Oleg V Tsodikov; Jeremy Kasanov; Tom Ellenberger; Gerhard Wagner; Tucker Collins Journal: Proc Natl Acad Sci U S A Date: 2007-03-05 Impact factor: 11.205
Authors: Fasséli Coulibaly; Elaine Chiu; Sascha Gutmann; Chitra Rajendran; Peter W Haebel; Keiko Ikeda; Hajime Mori; Vernon K Ward; Clemens Schulze-Briese; Peter Metcalf Journal: Proc Natl Acad Sci U S A Date: 2009-12-10 Impact factor: 11.205
Authors: Leo Y-C Lin; Bojana Rakic; Cecilia P C Chiu; Emilie Lameignere; Warren W Wakarchuk; Stephen G Withers; Natalie C J Strynadka Journal: J Biol Chem Date: 2011-08-31 Impact factor: 5.157
Authors: Juan D Chavez; Michelle Cilia; Chad R Weisbrod; Ho-Jong Ju; Jimmy K Eng; Stewart M Gray; James E Bruce Journal: J Proteome Res Date: 2012-03-30 Impact factor: 4.466
Authors: Yusong R Guo; Corey F Hryc; Joanita Jakana; Hongbing Jiang; David Wang; Wah Chiu; Weiwei Zhong; Yizhi J Tao Journal: Proc Natl Acad Sci U S A Date: 2014-08-18 Impact factor: 11.205
Authors: Catherine L Lawson; Shuchismita Dutta; John D Westbrook; Kim Henrick; Helen M Berman Journal: Acta Crystallogr D Biol Crystallogr Date: 2008-07-17