The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy.
The three dimensional (3D) structure of the ectodomain of the entire fusion mediating F protein from Sendai virus [MW (trimer) approximately 177 kDa] has been determined by cryoelectron microscopy of single molecules and subsequent 3D reconstruction at a resolution of approximately 16 A. The reconstruction, which has been obtained from the native, proteolytic processed fusion primed F1+F2 form, shows the protein protruding approximately 170 A out of the membrane in a homotrimeric association. It consists of a defined approximately 65 A wide distal head and an adjacent neck, which is connected to an 70 A 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.
Ludwig
Kai
K
Forschungszentrum für Elektronenmikroskopie, Freie Universität Berlin, Berlin, Germany.
Baljinnyam
Bolormaa
B
Herrmann
Andreas
A
Böttcher
Christoph
C
D000595:Amino Acid Sequence; D002460:Cell Line; D020285:Cryoelectron Microscopy; D006461:Hemolysis; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000648:ultrastructure
D014760:Viral Fusion Proteins