Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 113, Issue 33, Page 9351-9356, Year 2016
Publish date	Aug 16, 2016
Authors	Jiří Nováček / Marta Šiborová / Martin Benešík / Roman Pantůček / Jiří Doškař / Pavel Plevka /
PubMed Abstract	Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall ...Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with "double-layered" baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210° rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome's release.
External links	Proc Natl Acad Sci U S A / PubMed:27469164 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	3.8 - 28.6 Å
Structure data	EMDB-4003: tail tube of phi812-K420 bacteriophage with cotracted tail before genome release Method: EM (helical sym.) / Resolution: 10.4 Å 4051 5li2 EMDB-4051, PDB-5li2: bacteriophage phi812K1-420 tail sheath and tail tube protein in native tail Method: EM (helical sym.) / Resolution: 6.2 Å 4052 5li4 EMDB-4052, PDB-5li4: bacteriophage phi812K1-420 tail sheath protein after contraction Method: EM (helical sym.) / Resolution: 4.2 Å 4053 5lii EMDB-4053, PDB-5lii: bacteriophage phi812K1-420 major capsid protein Method: EM (single particle) / Resolution: 3.8 Å 4054 5lij EMDB-4054: bacteriophage phi812K1-420 major capsid protein PDB-5lij: polyalanine chain built in bacteriophage phi812K1-420 cement protein density map Method: EM (single particle) / Resolution: 4.2 Å EMDB-8201: Neck and connector complexes of native phi812-K420 bacteriophage, C1 symmetry reconstruction Method: EM (single particle) / Resolution: 28.6 Å EMDB-8202: Neck and connector complexes of native phi812-K420 bacteriophage, C5 symmetry reconstruction Method: EM (single particle) / Resolution: 27.1 Å EMDB-8203: Neck and connector complexes of native phi812-K420 bacteriophage, C6 symmetry reconstruction Method: EM (single particle) / Resolution: 28.3 Å EMDB-8204: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and full heads, C1 symmetry reconstruction Method: EM (single particle) / Resolution: 27.4 Å EMDB-8205: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and full heads, C5 symmetry reconstruction Method: EM (single particle) / Resolution: 28.2 Å EMDB-8206: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and full heads, C6 symmetry reconstruction Method: EM (single particle) / Resolution: 28.2 Å EMDB-8207: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and empty heads, C1 symmetry reconstruction Method: EM (single particle) / Resolution: 27.8 Å EMDB-8208: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and empty heads, C5 symmetry reconstruction Method: EM (single particle) / Resolution: 25.8 Å EMDB-8209: Neck and connector complexes of bacteriophage phi812-K420 with contracted tail and empty heads, C6 symmetry reconstruction Method: EM (single particle) / Resolution: 26.7 Å EMDB-8210: Native baseplate of bacteriophage phi812-K420 Method: EM (single particle) / Resolution: 13.4 Å EMDB-8211: Native baseplate of bacteriophage phi812-K420 with tail fibre in alternative conformation Method: EM (single particle) / Resolution: 18.4 Å EMDB-8212: baseplate of bacteriophage phi812-K420 in contracted state Method: EM (single particle) / Resolution: 10.8 Å EMDB-8213: receptor-tripod complex of bacteriophage phi812-K420 Method: EM (single particle) / Resolution: 7.9 Å EMDB-8214: receptor-tripod complex of bacteriophage phi812-K420 Method: EM (single particle) / Resolution: 10.2 Å EMDB-8304: phi812K1-420 capsid Method: EM (single particle) / Resolution: 5.1 Å
Source	staphylococcus phage 812 (virus) staphylococcus (bacteria)
Keywords	VIRAL PROTEIN / polyvalent staphylococcal bactoriophage / Myoviridae / tail sheath / tail contraction / VIRUS LIKE PARTICLE