2g2q
From Proteopedia
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The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond formation
Overview
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.
About this Structure
2G2Q is a Single protein structure of sequence from Vaccinia virus with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity., Su HP, Lin DY, Garboczi DN, J Virol. 2006 Aug;80(15):7706-13. PMID:16840349
Page seeded by OCA on Thu Feb 21 17:27:33 2008
Categories: Single protein | Vaccinia virus | Garboczi, D N. | Lin, D Y. | Su, H P. | SO4 | G4 | Orthopox | Oxidoreductase | Poxvirus | Thioredoxin-fold
