2ALA
Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.
2ALA の概要
エントリーDOI | 10.2210/pdb2ala/pdb |
関連するPDBエントリー | 1I9W 1RER |
分子名称 | Structural polyprotein (P130) (2 entities in total) |
機能のキーワード | envelope glycoprotein, membrane fusion, viral protein |
由来する生物種 | Semliki forest virus |
細胞内の位置 | 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 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 42690.13 |
構造登録者 | Roussel, A.,Lescar, J.,Vaney, M.C.,Wengler, G.,Wengler, G.,Rey, F.A. (登録日: 2005-08-05, 公開日: 2006-01-17, 最終更新日: 2024-11-06) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
構造検証レポート
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