3MAW
Structure of the Newcastle disease virus F protein in the post-fusion conformation
Summary for 3MAW
| Entry DOI | 10.2210/pdb3maw/pdb |
| Descriptor | Fusion glycoprotein F0, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | fusion protein, class i, paramyxovirus, glycoprotein, viral protein |
| Biological source | Newcastle disease virus (NDV) |
| Cellular location | Virion membrane; Single-pass type I membrane protein (By similarity): P12572 |
| Total number of polymer chains | 2 |
| Total formula weight | 104469.72 |
| Authors | Jardetzky, T.S.,Wen, X. (deposition date: 2010-03-24, release date: 2010-05-26, Last modification date: 2020-07-29) |
| Primary citation | Swanson, K.,Wen, X.,Leser, G.P.,Paterson, R.G.,Lamb, R.A.,Jardetzky, T.S. Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology, 402:372-379, 2010 Cited by PubMed Abstract: The paramyxovirus F protein is a class I viral membrane fusion protein which undergoes a significant refolding transition during virus entry. Previous studies of the Newcastle disease virus, human parainfluenza virus 3 and parainfluenza virus 5 F proteins revealed differences in the pre- and post-fusion structures. The NDV Queensland (Q) F structure lacked structural elements observed in the other two structures, which are key to the refolding and fusogenic activity of F. Here we present the NDV Australia-Victoria (AV) F protein post-fusion structure and provide EM evidence for its folding to a pre-fusion form. The NDV AV F structure contains heptad repeat elements missing in the previous NDV Q F structure, forming a post-fusion six-helix bundle (6HB) similar to the post-fusion hPIV3 F structure. Electrostatic and temperature factor analysis of the F structures points to regions of these proteins that may be functionally important in their membrane fusion activity. PubMed: 20439109DOI: 10.1016/j.virol.2010.03.050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
Download full validation report
