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The 3D structure of the fusion primed Sendai F‐protein determined by electron cryomicroscopy
Author(s) -
Ludwig Kai,
Baljinnyam Bolormaa,
Herrmann Andreas,
Böttcher Christoph
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg385
Subject(s) - humanities , art history , philosophy , history
The three dimensional (3D) structure of the ectodomain of the entire fusion mediating F protein from Sendai virus [MW (trimer) ∼177 kDa] has been determined by cryoelectron microscopy of single molecules and subsequent 3D reconstruction at a resolution of ∼16 Å. The reconstruction, which has been obtained from the native, proteolytic processed fusion primed F1+F2 form, shows the protein protruding ∼170 Å out of the membrane in a homotrimeric association. It consists of a defined ∼65 Å wide distal head and an adjacent neck, which is connected to an 70 Å elongated stalk. Although the overall shape appears to be similar to the recently reported X‐ray structure of the Newcastle disease virus F protein, a closer comparison reveals structural differences suggesting that the investigated Sendai F structure represents an advanced state towards the fusion active conformation.