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TitleMapping the structure and function of the E1 and E2 glycoproteins in alphaviruses.
Journal, issue, pagesStructure, Vol. 14, Issue 1, Page 63-73, Year 2006
Publish dateApr 13, 2006
AuthorsSuchetana Mukhopadhyay / Wei Zhang / Stefan Gabler / Paul R Chipman / Ellen G Strauss / James H Strauss / Timothy S Baker / Richard J Kuhn / Michael G Rossmann /
PubMed AbstractThe 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and ...The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion.
External linksStructure / PubMed:16407066 / PubMed Central
MethodsEM (single particle)
Resolution9.0 Å
Structure data

1121

1z8y

EMDB-1121: Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses.
PDB-1z8y: Mapping the E2 Glycoprotein of Alphaviruses
Method: EM (single particle) / Resolution: 9.0 Å

Source
  • sindbis virus
KeywordsVIRUS / icosahedral enveloped virus / Icosahedral virus

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