1dyl
From Proteopedia
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| , resolution 9.Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY
Overview
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.
About this Structure
1DYL is a Single protein structure of sequence from Semliki forest virus. Full crystallographic information is available from OCA.
Reference
Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus., Mancini EJ, Clarke M, Gowen BE, Rutten T, Fuller SD, Mol Cell. 2000 Feb;5(2):255-66. PMID:10882067
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