2g2q | pdb_00002g2q
The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond formation
Structural highlights
FunctionGLRX2_VACCW Glutaredoxin necessary for virion morphogenesis and virus replication. Functions as a thiol-disulfide transfer protein between membrane-associated A2.5 and substrates L1 or F9. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of E10, A2.5 and G4. Exhibit thioltransferase and dehydroascorbate reductase activities in vitro.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
