1DYL: 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

Citation:
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.
PDB ID: 1DYLDownload
MMDB ID: 14135
PDB Deposition Date: 2000/2/2
Updated in MMDB: 2007/10
Experimental Method:
electron microscopy
Resolution: 9  Å
Source Organism:
Similar Structures:
Biological Unit for 1DYL: 240-meric
Molecular Components in 1DYL
Label Count Molecule
Proteins (240 molecules)
240
Nucleocapsid Protein(Gene symbol: SFVgp2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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