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 of the T4 baseplate and its function in triggering sheath contraction.
Journal, issue, pages	Nature, Vol. 533, Issue 7603, Page 346-352, Year 2016
Publish date	May 19, 2016
Authors	Nicholas M I Taylor / Nikolai S Prokhorov / Ricardo C Guerrero-Ferreira / Mikhail M Shneider / Christopher Browning / Kenneth N Goldie / Henning Stahlberg / Petr G Leiman /
PubMed Abstract	Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This ...Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.
External links	Nature / PubMed:27193680
Methods	EM (single particle) / X-ray diffraction
Resolution	2.47 - 6.77 Å
Structure data	3374 5iv5 EMDB-3374, PDB-5iv5: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex Method: EM (single particle) / Resolution: 4.11 Å EMDB-3392: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex: locally masked refinement of the inner baseplate Method: EM (single particle) / Resolution: 3.83 Å EMDB-3393: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex: locally masked refinement of the intermediate baseplate Method: EM (single particle) / Resolution: 4.19 Å EMDB-3394: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex: locally masked refinement of the upper peripheral baseplate Method: EM (single particle) / Resolution: 4.55 Å EMDB-3395: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex: locally masked refinement of the lower peripheral baseplate Method: EM (single particle) / Resolution: 4.45 Å 3396 5iv7 EMDB-3396, PDB-5iv7: Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate Method: EM (single particle) / Resolution: 6.77 Å EMDB-3397: Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex: locally masked refinement of the tail tube Method: EM (single particle) / Resolution: 3.81 Å PDB-5iw9: Structure of bacteriophage T4 gp25, sheath polymerization initiator Method: X-RAY DIFFRACTION / Resolution: 2.47 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-FE: Unknown entry ChemComp-HOH: WATER
Source	enterobacteria phage t4 (virus)
Keywords	VIRAL PROTEIN / T4 / baseplate-tail tube complex / pre-attachment / bacteriophage / bacterial virus / hexagonal / membrane-piercing / cell attachment / infection / baseplate / post-attachment / star-shaped / hubless / contractile sheath / wedge / sheath polymerization