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-Structure paper
Title | Structural conservation of the myoviridae phage tail sheath protein fold. |
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Journal, issue, pages | Structure, Vol. 19, Issue 12, Page 1885-1894, Year 2011 |
Publish date | Dec 7, 2011 |
![]() | Anastasia A Aksyuk / Lidia P Kurochkina / Andrei Fokine / Farhad Forouhar / Vadim V Mesyanzhinov / Liang Tong / Michael G Rossmann / ![]() |
PubMed Abstract | Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The ...Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 Å resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 Å resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.3996 - 19.0 Å |
Structure data | EMDB-5331: The cryoEM structure of the bacteriophage phiKZ polysheath EMDB-5332: The cryoEM structure of the bacteriophage phiKZ polysheath ![]() PDB-3spe: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-GOL: ![]() ChemComp-HOH: |
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