2MM4

Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins

2MM4 の概要

• エントリーDOI: 10.2210/pdb2mm4/pdb
• NMR情報: BMRB: 19845
• 分子名称: Envelope small membrane protein (1 entity in total)
• 機能のキーワード: sars coronavirus, envelope protein, membrane protein, viral protein
• 由来する生物種: SARS coronavirus (Human SARS coronavirus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6313.60

構造登録者

Li, Y.,Surya, W.,Claudine, S.,Torres, J. (登録日: 2014-03-09, 公開日: 2014-04-02, 最終更新日: 2024-05-15)

主引用文献

Li, Y.,Surya, W.,Claudine, S.,Torres, J.
Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.
J.Biol.Chem., 289:12535-12549, 2014

PubMed Abstract: Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.

PubMed: 24668816
DOI: 10.1074/jbc.M114.560094

実験手法

SOLUTION NMR