3ES5
Crystal Structure of Partitivirus (PsV-F)
Summary for 3ES5
| Entry DOI | 10.2210/pdb3es5/pdb |
| Related | 1EJ6 1K4R 1M1C 1UF2 2BTV |
| Descriptor | Putative capsid protein (1 entity in total) |
| Functional Keywords | partitivirus, rna virus, double stranded rna virus, dsrna virus, t=2, "t=2" capsid, icosahedral virus, virus |
| Biological source | Penicillium stoloniferum virus F |
| Total number of polymer chains | 2 |
| Total formula weight | 93178.50 |
| Authors | Pan, J.,Dong, L.,Lin, L.,Ochoa, W.F.,Sinkovits, R.S.,Havens, W.M.,Nibert, M.L.,Baker, T.S.,Ghabrial, S.A.,Tao, Y.J. (deposition date: 2008-10-03, release date: 2009-03-10, Last modification date: 2024-04-03) |
| Primary citation | Pan, J.,Dong, L.,Lin, L.,Ochoa, W.F.,Sinkovits, R.S.,Havens, W.M.,Nibert, M.L.,Baker, T.S.,Ghabrial, S.A.,Tao, Y.J. Atomic structure reveals the unique capsid organization of a dsRNA virus. Proc.Natl.Acad.Sci.USA, 106:4225-4230, 2009 Cited by PubMed Abstract: For most dsRNA viruses, the genome-enclosing capsid comprises 120 copies of a single capsid protein (CP) organized into 60 icosahedrally equivalent dimers, generally identified as 2 nonsymmetricallyinteracting CP molecules with extensive lateral contacts. The crystal structure of a partitivirus, Penicillium stoloniferum virus F (PsV-F), reveals a different organization, in which the CP dimer is related by almost-perfect local 2-fold symmetry, forms prominent surface arches, and includes extensive structure swapping between the 2 subunits. An electron cryomicroscopy map of PsV-F shows that the disordered N terminus of each CP molecule interacts with the dsRNA genome and probably participates in its packaging or transcription. Intact PsV-F particles mediate semiconservative transcription, and transcripts are likely to exit through negatively charged channels at the icosahedral 5-fold axes. Other findings suggest that the PsV-F capsid is assembled from dimers of CP dimers, with an arrangement similar to flavivirus E glycoproteins. PubMed: 19246376DOI: 10.1073/pnas.0812071106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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