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	The molecular architecture of the bacteriophage T4 neck.
Journal, issue, pages	J Mol Biol, Vol. 425, Issue 10, Page 1731-1744, Year 2013
Publish date	May 27, 2013
Authors	Andrei Fokine / Zhihong Zhang / Shuji Kanamaru / Valorie D Bowman / Anastasia A Aksyuk / Fumio Arisaka / Venigalla B Rao / Michael G Rossmann /
PubMed Abstract	A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently ...A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers.
External links	J Mol Biol / PubMed:23434847 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.7001 - 25.0 Å
Structure data	5528 3j2o EMDB-5528: Cryo-EM structure of the contracted bacteriophage T4 tail containing the collar and whiskers made of fibritin molecules. PDB-3j2o: Model of the bacteriophage T4 fibritin based on the cryo-EM reconstruction of the contracted T4 tail containing the phage collar and whiskers Method: EM (single particle) / Resolution: 25.0 Å PDB-3j2m: The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the extended T4 tail Method: ELECTRON MICROSCOPY / Resolution: 15.0 Å PDB-3j2n: The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the contracted T4 tail Method: ELECTRON MICROSCOPY / Resolution: 16.0 Å PDB-4hud: Structure of the bacteriophage T4 tail terminator protein, gp15. Method: X-RAY DIFFRACTION / Resolution: 2.7001 Å PDB-4huh: Structure of the bacteriophage T4 tail terminator protein, gp15 (C-terminal truncation mutant 1-261). Method: X-RAY DIFFRACTION / Resolution: 3.2 Å
Chemicals	ChemComp-HOH: WATER / Water
Source	enterobacteria phage t4 (virus)
Keywords	VIRAL PROTEIN / bacteriophage T4 / phage tail terminator protein / phage sheath protein / phage neck / collar whiskers / fibritin / gpwac / gp15