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1P58

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

Summary for 1P58
Entry DOI10.2210/pdb1p58/pdb
Related1JCH 1K4R 1SVB
DescriptorMajor envelope protein E, Envelope protein M (2 entities in total)
Functional Keywordsflavivirus, flaviviridae, dengue virus, glycoprotein e from tick-borne encephalitis virus, membrane protein m, cryo-em, icosahedral virus, virus
Biological sourceDengue virus 2 Puerto Rico/PR159-S1/1969
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Total number of polymer chains6
Total formula weight188368.80
Authors
Zhang, W.,Chipman, P.R.,Corver, J.,Johnson, P.R.,Zhang, Y.,Mukhopadhyay, S.,Baker, T.S.,Strauss, J.H.,Rossmann, M.G.,Kuhn, R.J. (deposition date: 2003-04-25, release date: 2003-11-04, Last modification date: 2024-02-14)
Primary citationZhang, W.,Chipman, P.R.,Corver, J.,Johnson, P.R.,Zhang, Y.,Mukhopadhyay, S.,Baker, T.S.,Strauss, J.H.,Rossmann, M.G.,Kuhn, R.J.
Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
Nat.Struct.Biol., 10:907-912, 2003
Cited by
PubMed 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 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.
PubMed: 14528291
DOI: 10.1038/nsb990
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (9.5 Å)
Structure validation

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