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- PDB-4btg: Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1... -
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Basic information
Entry | Database: PDB / ID: 4btg | ||||||
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Title | Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution | ||||||
![]() | MAJOR INNER PROTEIN P1 | ||||||
![]() | VIRUS / CYSTOVIRIDAE / PROCAPSID STRUCTURE / FLEXIBLE FITTING | ||||||
Function / homology | : / Major inner capsid protein P1 / T=2 icosahedral viral capsid / viral inner capsid / viral nucleocapsid / RNA binding / identical protein binding / Major inner protein P1![]() | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.4 Å | ||||||
![]() | Nemecek, D. / Boura, E. / Wu, W. / Cheng, N. / Plevka, P. / Qiao, J. / Mindich, L. / Heymann, J.B. / Hurley, J.H. / Steven, A.C. | ||||||
![]() | ![]() Title: Subunit folds and maturation pathway of a dsRNA virus capsid. Authors: Daniel Nemecek / Evzen Boura / Weimin Wu / Naiqian Cheng / Pavel Plevka / Jian Qiao / Leonard Mindich / J Bernard Heymann / James H Hurley / Alasdair C Steven / ![]() 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 ...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. | ||||||
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Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 163.7 KB | Display | |
Data in CIF | ![]() | 216.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2364MC ![]() 4btqC ![]() 4k7hC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Assembly
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Symmetry | Point symmetry: (Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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