1dyl
From Proteopedia
(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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| - | [[Image:1dyl.gif|left|200px]]<br /><applet load="1dyl" size=" | + | [[Image:1dyl.gif|left|200px]]<br /><applet load="1dyl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dyl, resolution 9.Å" /> | caption="1dyl, resolution 9.Å" /> | ||
'''9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY'''<br /> | '''9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Semliki Forest virus serves as a paradigm for membrane fusion and | + | 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== | ==About this Structure== | ||
| - | 1DYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http:// | + | 1DYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clarke, M.]] | [[Category: Clarke, M.]] | ||
| - | [[Category: Fuller, S | + | [[Category: Fuller, S D.]] |
| - | [[Category: Gowen, B | + | [[Category: Gowen, B E.]] |
| - | [[Category: Mancini, E | + | [[Category: Mancini, E J.]] |
[[Category: Rutten, T.]] | [[Category: Rutten, T.]] | ||
[[Category: alphavirus]] | [[Category: alphavirus]] | ||
| Line 26: | Line 26: | ||
[[Category: sfv]] | [[Category: sfv]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:52 2008'' |
Revision as of 10:21, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 12:21:52 2008
