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5G47

Structure of Gc glycoprotein from severe fever with thrombocytopenia syndrome virus in the trimeric postfusion conformation

5G47 の概要
エントリーDOI10.2210/pdb5g47/pdb
分子名称SFTSV GC, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
機能のキーワードviral protein, phlebovirus, viral membrane fusion, glycoprotein, class ii viral fusion, bunyavirus, huaiyangshan virus, emerging virus, zoonosis
由来する生物種SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME VIRUS (SFTSV)
タンパク質・核酸の鎖数3
化学式量合計143862.69
構造登録者
Halldorsson, S.,Behrens, A.J.,Harlos, K.,Huiskonen, J.T.,Elliott, R.M.,Crispin, M.,Brennan, B.,Bowden, T.A. (登録日: 2016-05-05, 公開日: 2016-07-06, 最終更新日: 2024-10-09)
主引用文献Halldorsson, S.,Behrens, A.,Harlos, K.,Huiskonen, J.T.,Elliott, R.M.,Crispin, M.,Brennan, B.,Bowden, T.A.
Structure of a Phleboviral Envelope Glycoprotein Reveals a Consolidated Model of Membrane Fusion.
Proc.Natl.Acad.Sci.USA, 113:7154-, 2016
Cited by
PubMed Abstract: An emergent viral pathogen termed severe fever with thrombocytopenia syndrome virus (SFTSV) is responsible for thousands of clinical cases and associated fatalities in China, Japan, and South Korea. Akin to other phleboviruses, SFTSV relies on a viral glycoprotein, Gc, to catalyze the merger of endosomal host and viral membranes during cell entry. Here, we describe the postfusion structure of SFTSV Gc, revealing that the molecular transformations the phleboviral Gc undergoes upon host cell entry are conserved with otherwise unrelated alpha- and flaviviruses. By comparison of SFTSV Gc with that of the prefusion structure of the related Rift Valley fever virus, we show that these changes involve refolding of the protein into a trimeric state. Reverse genetics and rescue of site-directed histidine mutants enabled localization of histidines likely to be important for triggering this pH-dependent process. These data provide structural and functional evidence that the mechanism of phlebovirus-host cell fusion is conserved among genetically and patho-physiologically distinct viral pathogens.
PubMed: 27325770
DOI: 10.1073/PNAS.1603827113
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.45 Å)
構造検証レポート
Validation report summary of 5g47
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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