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	Assembly mechanism of the pleomorphic immature poxvirus scaffold.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 1704, Year 2022
Publish date	Mar 31, 2022
Authors	Jaekyung Hyun / Hideyuki Matsunami / Tae Gyun Kim / Matthias Wolf /
PubMed Abstract	In Vaccinia virus (VACV), the prototype poxvirus, scaffold protein D13 forms a honeycomb-like lattice on the viral membrane that results in formation of the pleomorphic immature virion (IV). The ...In Vaccinia virus (VACV), the prototype poxvirus, scaffold protein D13 forms a honeycomb-like lattice on the viral membrane that results in formation of the pleomorphic immature virion (IV). The structure of D13 is similar to those of major capsid proteins that readily form icosahedral capsids in nucleocytoplasmic large DNA viruses (NCLDVs). However, the detailed assembly mechanism of the nonicosahedral poxvirus scaffold has never been understood. Here we show the cryo-EM structures of the D13 trimer and scaffold intermediates produced in vitro. The structures reveal that the displacement of the short N-terminal α-helix is critical for initiation of D13 self-assembly. The continuous curvature of the IV is mediated by electrostatic interactions that induce torsion between trimers. The assembly mechanism explains the semiordered capsid-like arrangement of D13 that is distinct from icosahedral NCLDVs. Our structures explain how a single protein can self-assemble into different capsid morphologies and represent a local exception to the universal Caspar-Klug theory of quasi-equivalence.
External links	Nat Commun / PubMed:35361762 / PubMed Central
Methods	EM (single particle) / EM (helical sym.)
Resolution	2.25 - 7.33 Å
Structure data	31949 7vfd EMDB-31949, PDB-7vfd: Cryo-EM structure of Vaccinia virus scaffolding protein D13 Method: EM (single particle) / Resolution: 2.25 Å 31950 7vfe EMDB-31950, PDB-7vfe: Cryo-EM structure of Vaccinia virus scaffolding protein D13 with N-terminal polyhistidine tag Method: EM (single particle) / Resolution: 2.63 Å 31951 7vff EMDB-31951, PDB-7vff: Cryo-EM structure of Vaccinia virus scaffolding protein D13 with N-terminal 17 residue truncation Method: EM (single particle) / Resolution: 4.1 Å 31952 7vfg EMDB-31952, PDB-7vfg: Cryo-EM structure of Vaccinia virus scaffolding protein D13 trimer doublet Method: EM (single particle) / Resolution: 3.87 Å EMDB-31953: Cryo-EM structure of Vaccinia virus scaffolding protein D13 tubular assembly Method: EM (helical sym.) / Resolution: 7.33 Å 31954 7vfh EMDB-31954, PDB-7vfh: Cryo-EM structure of Vaccinia virus scaffolding protein D13 trimer sextet Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-HOH: WATER
Source	Vaccinia virus WR vaccinia virus (strain western reserve)
Keywords	VIRAL PROTEIN / Scaffold / capsid / double-jelly-roll