1P58

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

1P58 の概要

• エントリーDOI: 10.2210/pdb1p58/pdb
• 関連するPDBエントリー: 1JCH 1K4R 1SVB
• 分子名称: Major envelope protein E, Envelope protein M (2 entities in total)
• 機能のキーワード: flavivirus, flaviviridae, dengue virus, glycoprotein e from tick-borne encephalitis virus, membrane protein m, cryo-em, icosahedral virus, virus
• 由来する生物種: Dengue virus 2 Puerto Rico/PR159-S1/1969; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 188368.80

構造登録者

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. (登録日: 2003-04-25, 公開日: 2003-11-04, 最終更新日: 2024-02-14)

主引用文献

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.
Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
Nat.Struct.Biol., 10:907-912, 2003

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

実験手法

ELECTRON MICROSCOPY (9.5 Å)