1DYL

9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

Summary for 1DYL

• Entry DOI: 10.2210/pdb1dyl/pdb
• Related: 1VCP 1VCQ
• EMDB information: 1015
• Descriptor: NUCLEOCAPSID PROTEIN (1 entity in total)
• Functional Keywords: virus/viral protein, alphavirus, sfv, cryo-em, image reconstruction, enveloped virus, capsid protein, icosahedral virus, virus-viral protein complex
• Biological source: SEMLIKI FOREST VIRUS (SFV)
• Total number of polymer chains: 4
• Total formula weight: 65009.76

Authors

Mancini, E.J.,Clarke, M.,Gowen, B.E.,Rutten, T.,Fuller, S.D. (deposition date: 2000-02-02, release date: 2000-08-18, Last modification date: 2024-10-16)

Primary citation

Mancini, E.J.,Clarke, M.,Gowen, B.E.,Rutten, T.,Fuller, S.D.
Cryo-Electron Microscopy Reveals the Functional Organization of an Enveloped Virus, Semliki Forest Virus.
Mol.Cell, 5:255-266, 2000

PubMed Abstract: Semliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion structure to 9 A resolution. The improved resolution of this map reveals an N-terminal arm linking capsid subunits and defines the spike-capsid interaction sites. It illustrates the paired helical nature of the transmembrane segments and the elongated structures connecting them to the spike projecting domains. A 10 A diameter density in the fusion protein lines the cavity at the center of the spike. These clearly visible features combine with the variation in order between the layers to provide a framework for understanding the structural changes during the life cycle of an enveloped virus.

PubMed: 10882067
DOI: 10.1016/S1097-2765(00)80421-9

Experimental method

ELECTRON MICROSCOPY (9 Å)