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-Structure paper
タイトル | Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. |
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ジャーナル・号・ページ | Mol Cell, Vol. 5, Issue 2, Page 255-266, Year 2000 |
掲載日 | 2000年7月17日 |
著者 | E J Mancini / M Clarke / B E Gowen / T Rutten / S D Fuller / |
PubMed 要旨 | 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 ...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. |
リンク | Mol Cell / PubMed:10882067 |
手法 | EM (単粒子) |
解像度 | 9.0 Å |
構造データ | |
由来 |
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キーワード | VIRUS/VIRAL PROTEIN / ALPHAVIRUS / SFV / CRYO-EM / IMAGE RECONSTRUCTION / ENVELOPED VIRUS / CAPSID PROTEIN / ICOSAHEDRAL VIRUS / VIRUS-VIRAL PROTEIN complex |