4BTQ
Coordinates of the bacteriophage phi6 capsid subunits fitted into the cryoEM map EMD-1206
Summary for 4BTQ
Entry DOI | 10.2210/pdb4btq/pdb |
Related | 4BTG |
EMDB information | 1206 |
Descriptor | MAJOR INNER PROTEIN P1 (1 entity in total) |
Functional Keywords | viral protein, cystoviridae, procapsid structure, flexible fitting |
Biological source | PSEUDOMONAS PHAGE PHI6 |
Total number of polymer chains | 2 |
Total formula weight | 168327.34 |
Authors | Nemecek, D.,Boura, E.,Wu, W.,Cheng, N.,Plevka, P.,Qiao, J.,Mindich, L.,Heymann, J.B.,Hurley, J.H.,Steven, A.C. (deposition date: 2013-06-18, release date: 2013-12-11, Last modification date: 2024-05-08) |
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-, 2013 Cited by 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: 23891288DOI: 10.1016/J.STR.2013.06.007 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (7.5 Å) |
Structure validation
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