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Protein-RNA Interactions in an Icosahedral Virus at 3.0 Å Resolution

Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interacti...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1989-07, Vol.245 (4914), p.154-159
Main Authors: Chen, Zhongguo, Stauffacher, Cynthia, Li, Yunge, Schmidt, Tim, Bomu, Wu, Kamer, Greg, Shanks, Michael, Lomonossoff, George, Johnson, John E.
Format: Article
Language:English
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Summary:Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2749253