1SVF : PARAMYXOVIRUS SV5 FUSION PROTEIN CORE

  • Kent A. Baker (Contributor)
  • Rebecca Ellis Dutch (Contributor)
  • Robert A. Lamb (Department of Biochemistry) (Contributor)
  • Theodore S. Jardetzky (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.4
Classification:VIRAL PROTEIN
Release Date:1999-03-26
Deposition Date:1999-02-27
Revision Date:2008-04-26#2011-07-13
Molecular Weight:21145.28
Macromolecule Type:Protein
Residue Count:204
Atom Site Count:1434
DOI:10.2210/pdb1svf/pdb

Abstract:
Paramyxoviruses are responsible for significant human mortality and disease worldwide, but the molecular mechanisms underlying their entry into host cells remain poorly understood. We have solved the crystal structure of a fragment of the simian parainfluenza virus 5 fusion protein (SV5 F), revealing a 96 A long coiled coil surrounded by three antiparallel helices. This structure places the fusion and transmembrane anchor of SV5 F in close proximity with a large intervening domain at the opposite end of the coiled coil. Six amino acids, potentially part of the fusion peptide, form a segment of the central coiled coil, suggesting that this structure extends into the membrane. Deletion mutants of SV5 F indicate that putative flexible tethers between the coiled coil and the viral membrane are dispensable for fusion. The lack of flexible tethers may couple a final conformational change in the F protein directly to the fusion of two bilayers.
Date made available1999
PublisherRCSB-PDB

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