1I9W

CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS

Summary for 1I9W

• Entry DOI: 10.2210/pdb1i9w/pdb
• Descriptor: FUSION PROTEIN E1 (1 entity in total)
• Functional Keywords: envelope glycoprotein, virus, membrane fusion, viral protein
• Biological source: Semliki forest virus
• Cellular location: Capsid protein: Virion . p62: Virion membrane ; Single- pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Protein 6K: Host cell membrane ; Multi-pass membrane protein : P03315
• Total number of polymer chains: 1
• Total formula weight: 42619.05

Authors

Lescar, J.,Roussel, A.,Wien, M.W.,Navaza, J.,Fuller, S.D.,Wengler, G.,Wengler, G.,Rey, F.A. (deposition date: 2001-03-21, release date: 2002-04-06, Last modification date: 2024-02-07)

Primary citation

Lescar, J.,Roussel, A.,Wien, M.W.,Navaza, J.,Fuller, S.D.,Wengler, G.,Wengler, G.,Rey, F.A.
The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH.
Cell(Cambridge,Mass.), 105:137-148, 2001

PubMed Abstract: Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce a new class of membrane fusion proteins which display lateral interactions to induce the necessary curvature and direct budding of closed particles. The resulting surface protein lattice is primed to cause membrane fusion when exposed to the acidic environment of the endosome.

PubMed: 11301009
DOI: 10.1016/S0092-8674(01)00303-8

Experimental method

X-RAY DIFFRACTION (3 Å)