1dyl: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dyl.gif|left|200px]]<br /><applet load="1dyl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dyl, resolution 9.&Aring;" />
caption="1dyl, resolution 9.&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DYL OCA].  
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.D.]]
[[Category: Fuller, S D.]]
[[Category: Gowen, B.E.]]
[[Category: Gowen, B E.]]
[[Category: Mancini, E.J.]]
[[Category: Mancini, E J.]]
[[Category: Rutten, T.]]
[[Category: Rutten, T.]]
[[Category: alphavirus]]
[[Category: alphavirus]]
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[[Category: sfv]]
[[Category: sfv]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:41:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:52 2008''