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-Structure paper
タイトル | Subunit folds and maturation pathway of a dsRNA virus capsid. |
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ジャーナル・号・ページ | Structure, Vol. 21, Issue 8, Page 1374-1383, Year 2013 |
掲載日 | 2013年8月6日 |
著者 | Daniel Nemecek / Evzen Boura / Weimin Wu / Naiqian Cheng / Pavel Plevka / Jian Qiao / Leonard Mindich / J Bernard Heymann / James H Hurley / Alasdair C Steven / |
PubMed 要旨 | The cystovirus ϕ6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits ...The cystovirus ϕ6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. ϕ6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an α-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine. |
リンク | Structure / PubMed:23891288 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.5964 - 7.5 Å |
構造データ | EMDB-2364: CryoEM reconstruction of the bacteriophage phi6 procapsid to the near-atomic resolution PDB-4btq: PDB-4k7h: |
由来 |
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キーワード | VIRUS / CYSTOVIRIDAE / PROCAPSID STRUCTURE / FLEXIBLE FITTING / VIRAL PROTEIN / major capsid protein |