The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy

EMBO J. 2003 Aug 1;22(15):3761-71. doi: 10.1093/emboj/cdg385.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Cryoelectron Microscopy
  • Hemolysis
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / ultrastructure

Substances

  • Viral Fusion Proteins