1p58 | pdb_00001p58

File:1p58.gif

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Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction

Overview

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 A 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 alpha-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 alpha-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.

About this Structure

1P58 is a Protein complex structure of sequences from Dengue virus type 3. Full crystallographic information is available from OCA.

Reference

Visualization of membrane protein domains by cryo-electron microscopy of dengue virus., Zhang W, Chipman PR, Corver J, Johnson PR, Zhang Y, Mukhopadhyay S, Baker TS, Strauss JH, Rossmann MG, Kuhn RJ, Nat Struct Biol. 2003 Nov;10(11):907-12. Epub 2003 Oct 5. PMID:14528291

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