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5CW0

Investigation of RNA structure in satellite panicum mosaic virus

Summary for 5CW0
Entry DOI10.2210/pdb5cw0/pdb
Related1STM
DescriptorCoat protein (1 entity in total)
Functional Keywordscapsid protein, satellite virus, virus
Biological sourceSatellite panicum mosaic virus (SPMV)
Total number of polymer chains1
Total formula weight16983.16
Authors
Makino, D.L.,Day, J.,Larson, S.B.,McPherson, A. (deposition date: 2015-07-27, release date: 2017-10-11, Last modification date: 2023-09-27)
Primary citationMakino, D.L.,Day, J.,Larson, S.B.,McPherson, A.
Investigation of RNA structure in satellite panicum mosaic virus.
Virology, 351:420-431, 2006
Cited by
PubMed Abstract: Three new crystal forms of satellite panicum mosaic virus (SPMV) were grown and their structures solved from X-ray diffraction data using molecular replacement techniques. The crystals were grown under conditions of pH and ionic strength that were appreciably different then those used for the original structure determination. In rhombohedral crystals grown at pH 8.5 and low ionic strength PEG 3350 solutions, Fourier syntheses revealed segments, ten amino acid residues long, of amino-terminal polypeptides not previously seen, as well as masses of electron density within concavities on the interior of the capsid, which appeared in the neighborhoods of icosahedral five- and threefold axes. The densities were compatible with secondary structural domains of RNA, and they included a segment of double helical RNA of about four to five base pairs oriented, at least approximately, along the fivefold axes. The distribution of RNA observed for SPMV appears to be distinctly different than the encapsidated nucleic acid conformation previously suggested for another satellite virus, satellite tobacco mosaic virus. This study further shows that analysis of viruses in crystals grown under different chemical conditions may reveal additional information regarding the structure of encapsidated RNA.
PubMed: 16677679
DOI: 10.1016/j.virol.2006.03.028
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.6 Å)
Structure validation

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数据于2025-06-18公开中

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