2ALA
Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.
Summary for 2ALA
| Entry DOI | 10.2210/pdb2ala/pdb |
| Related | 1I9W 1RER |
| Descriptor | Structural polyprotein (P130) (2 entities in total) |
| Functional Keywords | envelope glycoprotein, membrane fusion, viral protein |
| Biological source | Semliki forest virus |
| Cellular location | Capsid protein: Virion (By similarity). p62: Virion membrane; Single-pass type I membrane protein (By similarity). E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). 6K protein: Host cell membrane; Multi-pass membrane protein (By similarity): P03315 |
| Total number of polymer chains | 1 |
| Total formula weight | 42690.13 |
| Authors | Roussel, A.,Lescar, J.,Vaney, M.C.,Wengler, G.,Wengler, G.,Rey, F.A. (deposition date: 2005-08-05, release date: 2006-01-17, Last modification date: 2024-11-06) |
| Primary citation | Roussel, A.,Lescar, J.,Vaney, M.C.,Wengler, G.,Wengler, G.,Rey, F.A. Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure, 14:75-86, 2006 Cited by PubMed Abstract: 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. PubMed: 16407067DOI: 10.1016/j.str.2005.09.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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