2B9B

Structure of the Parainfluenza Virus 5 F Protein in its Metastable, Pre-fusion Conformation

Summary for 2B9B

• Entry DOI: 10.2210/pdb2b9b/pdb
• Descriptor: Fusion glycoprotein F0, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: fusion protein, pre-fusion conformation, viral protein
• Biological source: Simian virus 5
• Cellular location: Virion membrane; Single-pass type I membrane protein (By similarity): P04849
• Total number of polymer chains: 3
• Total formula weight: 163300.33

Authors

Yin, H.-S.,Wen, X.,Paterson, R.G.,Lamb, R.A.,Jardetzky, T.S. (deposition date: 2005-10-11, release date: 2006-01-24, Last modification date: 2024-11-20)

Primary citation

Yin, H.-S.,Wen, X.,Paterson, R.G.,Lamb, R.A.,Jardetzky, T.S.
Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
Nature, 439:38-44, 2006

PubMed Abstract: Enveloped viruses have evolved complex glycoprotein machinery that drives the fusion of viral and cellular membranes, permitting entry of the viral genome into the cell. For the paramyxoviruses, the fusion (F) protein catalyses this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. Here we report the crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation, stabilized by the addition of a carboxy-terminal trimerization domain. The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure. The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the F protein.

PubMed: 16397490
DOI: 10.1038/nature04322

Experimental method

X-RAY DIFFRACTION (2.85 Å)