5MF1
Crystal structure of a C-terminally truncated trimeric ectodomain of the Chlamydomonas reinhardtii gamete fusion protein HAP2
5MF1 の概要
エントリーDOI | 10.2210/pdb5mf1/pdb |
分子名称 | Fusion protein HAP2/GCS1, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-galactopyranose (3 entities in total) |
機能のキーワード | class ii membrane fusion protein, type i transmembrane protein, glycoprotein, membrane protein |
由来する生物種 | Chlamydomonas reinhardtii |
細胞内の位置 | Cell membrane ; Single- pass type I membrane protein : A4GRC6 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 194586.68 |
構造登録者 | |
主引用文献 | Fedry, J.,Liu, Y.,Pehau-Arnaudet, G.,Pei, J.,Li, W.,Tortorici, M.A.,Traincard, F.,Meola, A.,Bricogne, G.,Grishin, N.V.,Snell, W.J.,Rey, F.A.,Krey, T. The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein. Cell, 168:904-915.e10, 2017 Cited by PubMed Abstract: Sexual reproduction is almost universal in eukaryotic life and involves the fusion of male and female haploid gametes into a diploid cell. The sperm-restricted single-pass transmembrane protein HAP2-GCS1 has been postulated to function in membrane merger. Its presence in the major eukaryotic taxa-animals, plants, and protists (including important human pathogens like Plasmodium)-suggests that many eukaryotic organisms share a common gamete fusion mechanism. Here, we report combined bioinformatic, biochemical, mutational, and X-ray crystallographic studies on the unicellular alga Chlamydomonas reinhardtii HAP2 that reveal homology to class II viral membrane fusion proteins. We further show that targeting the segment corresponding to the fusion loop by mutagenesis or by antibodies blocks gamete fusion. These results demonstrate that HAP2 is the gamete fusogen and suggest a mechanism of action akin to viral fusion, indicating a way to block Plasmodium transmission and highlighting the impact of virus-cell genetic exchanges on the evolution of eukaryotic life. PubMed: 28235200DOI: 10.1016/j.cell.2017.01.024 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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