2G2Q

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

Summary for 2G2Q

• Entry DOI: 10.2210/pdb2g2q/pdb
• Descriptor: Glutaredoxin-2, SULFATE ION (3 entities in total)
• Functional Keywords: thioredoxin-fold, oxidoreductase, poxvirus, vaccinia virus, orthopox, g4
• Biological source: Vaccinia virus
• Cellular location: Host cytoplasm: P68460
• Total number of polymer chains: 3
• Total formula weight: 42620.43

Authors

Su, H.P.,Lin, D.Y.,Garboczi, D.N. (deposition date: 2006-02-16, release date: 2006-08-01, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)