1PGW

BEAN POD MOTTLE VIRUS (BPMV), TOP COMPONENT

Summary for 1PGW

• Entry DOI: 10.2210/pdb1pgw/pdb
• Related: 1BMV 1NY7 1PGL
• Descriptor: BEAN POD MOTTLE VIRUS SMALL (S) SUBUNIT, BEAN POD MOTTLE VIRUS LARGE (L) SUBUNIT (3 entities in total)
• Functional Keywords: comovirus, virus, viral coat protein, bean pod mottle virus (bpmv), icosahedral virus
• Biological source: Bean-pod mottle virus (strain Kentucky G7); More
• Cellular location: Movement protein: Host cell junction, host plasmodesma . Large coat protein: Virion : P23009 P23009
• Total number of polymer chains: 2
• Total formula weight: 59314.04

Authors

Lin, T.,Cavarelli, J.,Johnson, J.E. (deposition date: 2003-05-28, release date: 2003-11-18, Last modification date: 2024-04-03)

Primary citation

Lin, T.,Cavarelli, J.,Johnson, J.E.
Evidence for assembly-dependent folding of protein and RNA in an icosahedral virus.
Virology, 314:26-33, 2003

PubMed Abstract: Ordered nucleic acid in an icosahedral virus was first visualized in the X-ray structure of the Picorna-like plant virus, Bean pod mottle virus (BPMV). Virus particles containing the 3500 nucleotide segment of the BPMV bipartite RNA genome (middle component) had nearly 20% of the genome ordered. Here we report the refined structures of the middle component, bottom component (particles containing the 5800 nucleotide segment of the genome), and top component (empty particles of BPMV capsid protein). The bottom component particles contain ordered RNA in the same location as middle component. Although the ordered RNA density in both nucleoprotein particles is the average of the contents of 60 icosahedral asymmetric units, both nucleoprotein components show that the base density for the first two nucleotides is predominantly purine, while the next five appear to be predominantly pyrimidine. The empty capsid demonstrates that RNA dictates the order of the N-terminal 19 residues of the large subunit because these residues are invisible in the top component.

PubMed: 14517057
DOI: 10.1016/S0042-6822(03)00457-4

Experimental method

X-RAY DIFFRACTION (2.9 Å)