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2g2q
From Proteopedia
Revision as of 09:00, 30 September 2014 by OCA (Talk | contribs)
2g2q is a 3 chain structure with sequence from Vaccinia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Su HP, Lin DY, Garboczi DN. The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity. J Virol. 2006 Aug;80(15):7706-13. PMID:16840349 doi:80/15/7706
