4K7H

Major capsid protein P1 of the Pseudomonas phage phi6

Summary for 4K7H

• Entry DOI: 10.2210/pdb4k7h/pdb
• Descriptor: Major inner protein P1 (1 entity in total)
• Functional Keywords: major capsid protein, viral protein
• Biological source: Pseudomonas phage phi6
• Cellular location: Virion: P11126
• Total number of polymer chains: 5
• Total formula weight: 429177.26

Authors

Boura, E.,Nemecek, D.,Plevka, P.,Steven, C.A.,Hurley, J.H. (deposition date: 2013-04-17, release date: 2013-08-14, Last modification date: 2024-04-03)

Primary citation

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, 21:1374-1383, 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

Experimental method

X-RAY DIFFRACTION (3.5964 Å)