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Yorodumi- PDB-4an5: Capsid structure and its Stability at the Late Stages of Bacterio... -
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-Basic information
Entry | Database: PDB / ID: 4an5 | ||||||
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Title | Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly | ||||||
Components | COAT PROTEIN | ||||||
Keywords | VIRUS / BACTERIOPHAGE CAPSID SPP1 | ||||||
Function / homology | Major capsid protein 13-like / Major capsid protein 13-like / T=7 icosahedral viral capsid / viral capsid / Major capsid protein Function and homology information | ||||||
Biological species | BACILLUS PHAGE SPP1 (virus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.8 Å | ||||||
Model type details | CA ATOMS ONLY, CHAIN A, B, C, D, E, F, G | ||||||
Authors | White, H.E. / Sherman, M.B. / Brasiles, S. / Jacquet, E. / Seavers, P. / Tavares, P. / Orlova, E.V. | ||||||
Citation | Journal: J Virol / Year: 2012 Title: Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly. Authors: Helen E White / Michael B Sherman / Sandrine Brasilès / Eric Jacquet / Philippa Seavers / Paulo Tavares / Elena V Orlova / Abstract: The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major ...The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12, which are organized in a T=7 lattice. DNA is arranged in layers with a distance of ~24.5 Å. gp12 forms spikes that are anchored at the center of gp13 hexamers. In a gp12-deficient mutant, the centers of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudoatomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between the thermostability of the capsid and those of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle coevolved toward high robustness. | ||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 4an5.cif.gz | 65.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4an5.ent.gz | 41.9 KB | Display | PDB format |
PDBx/mmJSON format | 4an5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4an5_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 4an5_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 4an5_validation.xml.gz | 27.5 KB | Display | |
Data in CIF | 4an5_validation.cif.gz | 39.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/4an5 ftp://data.pdbj.org/pub/pdb/validation_reports/an/4an5 | HTTPS FTP |
-Related structure data
Related structure data | 2049MC 2050C 2051C 2052C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
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Symmetry | Point symmetry: (Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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