1ZTM

Structure of the Uncleaved Paramyxovirus (hPIV3) Fusion Protein

Summary for 1ZTM

• Entry DOI: 10.2210/pdb1ztm/pdb
• Descriptor: Fusion glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: fusion protein, 6-helix bundle, trimer, post-fusion, viral protein
• Biological source: Human parainfluenza virus 3
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P06828
• Total number of polymer chains: 3
• Total formula weight: 163175.92

Authors

Yin, H.S.,Paterson, R.G.,Wen, X.,Lamb, R.A.,Jardetzky, T.S. (deposition date: 2005-05-27, release date: 2005-07-19, Last modification date: 2024-10-09)

Primary citation

Yin, H.S.,Paterson, R.G.,Wen, X.,Lamb, R.A.,Jardetzky, T.S.
Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
Proc.Natl.Acad.Sci.USA, 102:9288-9293, 2005

PubMed Abstract: Class I viral fusion proteins share common mechanistic and structural features but little sequence similarity. Structural insights into the protein conformational changes associated with membrane fusion are based largely on studies of the influenza virus hemagglutinin in pre- and postfusion conformations. Here, we present the crystal structure of the secreted, uncleaved ectodomain of the paramyxovirus, human parainfluenza virus 3 fusion (F) protein, a member of the class I viral fusion protein group. The secreted human parainfluenza virus 3 F forms a trimer with distinct head, neck, and stalk regions. Unexpectedly, the structure reveals a six-helix bundle associated with the postfusion form of F, suggesting that the anchor-minus ectodomain adopts a conformation largely similar to the postfusion state. The transmembrane anchor domains of F may therefore profoundly influence the folding energetics that establish and maintain a metastable, prefusion state.

PubMed: 15964978
DOI: 10.1073/pnas.0503989102

Experimental method

X-RAY DIFFRACTION (3.05 Å)