1BMV

PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION

Summary for 1BMV

• Entry DOI: 10.2210/pdb1bmv/pdb
• Descriptor: RNA (5'-R(*GP*GP*UP*CP*AP*AP*AP*AP*UP*GP*C)-3'), PROTEIN (ICOSAHEDRAL VIRUS - A DOMAIN), PROTEIN (ICOSAHEDRAL VIRUS - B AND C DOMAIN) (3 entities in total)
• Functional Keywords: protein-rna complex, single strand, icosahedral virus, virus-rna complex, virus/rna
• Biological source: Bean pod mottle virus; More
• Cellular location: Movement protein: Host cell junction, host plasmodesma (By similarity). Large coat protein: Virion (Potential): P23009 P23009
• Total number of polymer chains: 3
• Total formula weight: 66668.33

Authors

Chen, Z.,Stauffacher, C.,Li, Y.,Schmidt, T.,Bomu, W.,Kamer, G.,Shanks, M.,Lomonossoff, G.,Johnson, J.E. (deposition date: 1989-10-09, release date: 1989-10-09, Last modification date: 2024-05-22)

Primary citation

Chen, Z.G.,Stauffacher, C.,Li, Y.,Schmidt, T.,Bomu, W.,Kamer, G.,Shanks, M.,Lomonossoff, G.,Johnson, J.E.
Protein-RNA interactions in an icosahedral virus at 3.0 A resolution.
Science, 245:154-159, 1989

PubMed Abstract: 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.

PubMed: 2749253

Experimental method

X-RAY DIFFRACTION (3 Å)