1dyl
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(New page: 200px<br /><applet load="1dyl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dyl, resolution 9.Å" /> '''9 ANGSTROM RESOLUTION ...)
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Revision as of 11:33, 20 November 2007
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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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