3ES5

Crystal Structure of Partitivirus (PsV-F)

3ES5 の概要

• エントリーDOI: 10.2210/pdb3es5/pdb
• 関連するPDBエントリー: 1EJ6 1K4R 1M1C 1UF2 2BTV
• 分子名称: Putative capsid protein (1 entity in total)
• 機能のキーワード: partitivirus, rna virus, double stranded rna virus, dsrna virus, t=2, "t=2" capsid, icosahedral virus, virus
• 由来する生物種: Penicillium stoloniferum virus F
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93178.50

構造登録者

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. (登録日: 2008-10-03, 公開日: 2009-03-10, 最終更新日: 2024-04-03)

主引用文献

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

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: 19246376
DOI: 10.1073/pnas.0812071106

実験手法

X-RAY DIFFRACTION (3.3 Å)