2ala

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ala FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ala OCA], [http://www.ebi.ac.uk/pdbsum/2ala PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ala RCSB]</span>
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[[Category: viral protein]]
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Revision as of 22:54, 30 March 2008


PDB ID 2ala

Drag the structure with the mouse to rotate
, resolution 3.00Å
Related: 1I9W, 1RER


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.


Overview

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.

About this Structure

2ALA is a Single protein structure of sequence from Semliki forest virus. Full crystallographic information is available from OCA.

Reference

Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus., Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, Rey FA, Structure. 2006 Jan;14(1):75-86. PMID:16407067

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