3DUZ

Crystal structure of the postfusion form of baculovirus fusion protein GP64

Summary for 3DUZ

• Entry DOI: 10.2210/pdb3duz/pdb
• Descriptor: Major envelope glycoprotein, MERCURY (II) ION (2 entities in total)
• Functional Keywords: fusion protein, coiled-coil, fusion peptide, trimer, viral, glycoprotein, lipoprotein, membrane, palmitate, phosphoprotein, transmembrane, virion, viral protein
• Biological source: Autographa californica nuclear polyhedrosis virus
• Cellular location: Virion membrane; Single-pass membrane protein (Potential): P17501
• Total number of polymer chains: 1
• Total formula weight: 56875.71

Authors

Kadlec, J.,Loureiro, S.,Abrescia, N.G.A.,Jones, I.M.,Stuart, D.I. (deposition date: 2008-07-18, release date: 2008-09-16, Last modification date: 2024-10-30)

Primary citation

Kadlec, J.,Loureiro, S.,Abrescia, N.G.,Stuart, D.I.,Jones, I.M.
The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines.
Nat.Struct.Mol.Biol., 15:1024-1030, 2008

PubMed Abstract: Viral fusion proteins mediate the merger of host and viral membranes during cell entry for all enveloped viruses. Baculovirus glycoprotein gp64 (gp64) is unusual in promoting entry into both insect and mammalian cells and is distinct from established class I and class II fusion proteins. We report the crystal structure of its postfusion form, which explains a number of gp64's biological properties including its cellular promiscuity, identifies the fusion peptides and shows it to be the third representative of a new class (III) of fusion proteins with unexpected structural homology with vesicular stomatitis virus G and herpes simplex virus type 1 gB proteins. We show that domains of class III proteins have counterparts in both class I and II proteins, suggesting that all these viral fusion machines are structurally more related than previously thought.

PubMed: 18776902
DOI: 10.1038/nsmb.1484

Experimental method

X-RAY DIFFRACTION (2.95 Å)