2G2Q

The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond formation

2G2Q の概要

• エントリーDOI: 10.2210/pdb2g2q/pdb
• 分子名称: Glutaredoxin-2, SULFATE ION (3 entities in total)
• 機能のキーワード: thioredoxin-fold, oxidoreductase, poxvirus, vaccinia virus, orthopox, g4
• 由来する生物種: Vaccinia virus
• 細胞内の位置: Host cytoplasm: P68460
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 42620.43

構造登録者

Su, H.P.,Lin, D.Y.,Garboczi, D.N. (登録日: 2006-02-16, 公開日: 2006-08-01, 最終更新日: 2024-10-30)

主引用文献

Su, H.P.,Lin, D.Y.,Garboczi, D.N.
The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity.
J.Virol., 80:7706-7713, 2006

PubMed Abstract: The possibility of the release of smallpox virus into a predominantly nonimmunized population highlights the importance of understanding poxvirus biology. Poxviruses encode a conserved pathway that is required to oxidize disulfide bonds in nascent viral proteins that fold in the reducing environment of the eukaryotic host cytoplasm. We present the structure of the last enzyme of the vaccinia virus pathway, G4, which is almost identical in smallpox virus. G4 catalyzes the formation of disulfide bonds in proteins that are critical for virus maturation and host cell infection. G4 contains a thioredoxin fold and a Cys-X-X-Cys active site. In solution, G4 monomers and dimers are observed. In the crystal, G4 is found as a dimer that buries 4,500 A(2) in the interface and occludes the active site, which could protect the reactive disulfide from reduction in the cytoplasm. The structure serves as a model for drug design targeting viral disulfide bond formation.

PubMed: 16840349
DOI: 10.1128/JVI.00521-06

実験手法

X-RAY DIFFRACTION (2.5 Å)