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4BTQ

Coordinates of the bacteriophage phi6 capsid subunits fitted into the cryoEM map EMD-1206

Summary for 4BTQ
Entry DOI10.2210/pdb4btq/pdb
Related4BTG
EMDB information1206
DescriptorMAJOR INNER PROTEIN P1 (1 entity in total)
Functional Keywordsviral protein, cystoviridae, procapsid structure, flexible fitting
Biological sourcePSEUDOMONAS PHAGE PHI6
Total number of polymer chains2
Total formula weight168327.34
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 citationNemecek, 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: 23891288
DOI: 10.1016/J.STR.2013.06.007
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.5 Å)
Structure validation

226707

数据于2024-10-30公开中

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