1dyl

9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

Structural highlights 1dyl is a 4 chain structure with sequence from Semliki forest virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1vcq, 1vcp Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

spinqualitylabelsall models 1dyl, resolution 9.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image