4BTG

Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution

4BTG の概要

• エントリーDOI: 10.2210/pdb4btg/pdb
• EMDBエントリー: 2364
• 分子名称: MAJOR INNER PROTEIN P1 (1 entity in total)
• 機能のキーワード: virus, cystoviridae, procapsid structure, flexible fitting
• 由来する生物種: PSEUDOMONAS PHAGE PHI6
• 細胞内の位置: Virion: P11126
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 168327.34

構造登録者

Nemecek, D.,Boura, E.,Wu, W.,Cheng, N.,Plevka, P.,Qiao, J.,Mindich, L.,Heymann, J.B.,Hurley, J.H.,Steven, A.C. (登録日: 2013-06-17, 公開日: 2013-08-14, 最終更新日: 2024-05-08)

主引用文献

Nemecek, D.,Boura, E.,Wu, W.,Cheng, N.,Plevka, P.,Qiao, J.,Mindich, L.,Heymann, J.B.,Hurley, J.H.,Steven, A.C.
Subunit Folds and Maturation Pathway of a Dsrna Virus Capsid.
Structure, 21:1374-, 2013

PubMed Abstract: 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.

PubMed: 23891288
DOI: 10.1016/J.STR.2013.06.007

実験手法

ELECTRON MICROSCOPY (4.4 Å)