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	An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 756, Year 2024
Publish date	Jan 26, 2024
Authors	Ravi R Sonani / Lee K Palmer / Nathaniel C Esteves / Abigail A Horton / Amanda L Sebastian / Rebecca J Kelly / Fengbin Wang / Mark A B Kreutzberger / William K Russell / Petr G Leiman / Birgit E Scharf / Edward H Egelman /
PubMed Abstract	A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, ...A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail of Agrobacterium tumefaciens bacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism.
External links	Nat Commun / PubMed:38272938 / PubMed Central
Methods	EM (single particle) / EM (helical sym.)
Resolution	2.9 - 3.3 Å
Structure data	29353 8fop EMDB-29353, PDB-8fop: Structure of Agrobacterium tumefaciens bacteriophage Milano curved tail Method: EM (single particle) / Resolution: 3.2 Å 29354 8fou EMDB-29354, PDB-8fou: Structure of Agrobacterium tumefaciens bacteriophage Milano contracted tail-tube Method: EM (helical sym.) / Resolution: 3.3 Å 29355 8foy EMDB-29355, PDB-8foy: Structure of Agrobacterium tumefaciens bacteriophage Milano contracted tail-sheath Method: EM (helical sym.) / Resolution: 2.9 Å 29383 8fqc EMDB-29383, PDB-8fqc: Structure of baseplate with receptor binding complex of Agrobacterium phage Milano Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-FE: Unknown entry
Source	agrobacterium phage milano (virus)
Keywords	VIRUS / Myophage / redox trigger / disulfides