5J9H
Crystal structure of Glycoprotein C from Puumala virus in the post-fusion conformation (pH 8.0)
5J9H の概要
エントリーDOI | 10.2210/pdb5j9h/pdb |
関連するPDBエントリー | 5J81 |
分子名称 | Envelopment polyprotein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
機能のキーワード | hantavirus, membrane fusion, conformational changes, enveloped viruses, virus entry, viral protein |
由来する生物種 | Puumala virus (strain P360) |
細胞内の位置 | Glycoprotein N: Virion membrane . Glycoprotein C: Virion membrane : P41266 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 49668.91 |
構造登録者 | |
主引用文献 | Willensky, S.,Bar-Rogovsky, H.,Bignon, E.A.,Tischler, N.D.,Modis, Y.,Dessau, M. Crystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformation. Plos Pathog., 12:e1005948-e1005948, 2016 Cited by PubMed Abstract: Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens. PubMed: 27783673DOI: 10.1371/journal.ppat.1005948 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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