2ALA: Crystal Structure Of The Semliki Forest Virus Envelope Protein E1 In Its Monomeric Conformation

Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.
PDB ID: 2ALADownload
MMDB ID: 37067
PDB Deposition Date: 2005/8/5
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 2ALA: monomeric; determined by author
Molecular Components in 2ALA
Label Count Molecule
Protein (1 molecule)
Structural Polyprotein (P130)(Gene symbol: SFVgp2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB