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- Title
Visualization of membrane protein domains by cryo-electron microscopy of dengue virus.
- Authors
Zhang, Wei; Chipman, Paul R; Corver, Jeroen; Johnson, Peter R; Zhang, Ying; Mukhopadhyay, Suchetana; Baker, Timothy S; Strauss, James H; Rossmann, Michael G; Kuhn, Richard J
- Abstract
Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 Å by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope (E) and 180 membrane (M) proteins in the lipid envelope. The a-helical 'stem' regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The 'anchor' regions of E and the M proteins each form antiparallel E-E and M-M transmembrane a-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus.
- Subjects
MEMBRANE proteins; DENGUE viruses; BIOLOGICAL membranes; PROTEINS; FLAVIVIRUSES; MICROSCOPY
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 11, p907
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb990