2g2q
From Proteopedia
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|PDB= 2g2q |SIZE=350|CAPTION= <scene name='initialview01'>2g2q</scene>, resolution 2.500Å | |PDB= 2g2q |SIZE=350|CAPTION= <scene name='initialview01'>2g2q</scene>, resolution 2.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= g4l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus]) | |GENE= g4l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g2q OCA], [http://www.ebi.ac.uk/pdbsum/2g2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g2q RCSB]</span> | ||
}} | }} | ||
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[[Category: Lin, D Y.]] | [[Category: Lin, D Y.]] | ||
[[Category: Su, H P.]] | [[Category: Su, H P.]] | ||
| - | [[Category: SO4]] | ||
[[Category: g4]] | [[Category: g4]] | ||
[[Category: orthopox]] | [[Category: orthopox]] | ||
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[[Category: vaccinia virus]] | [[Category: vaccinia virus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:11:01 2008'' |
Revision as of 00:11, 31 March 2008
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| , resolution 2.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | g4l (Vaccinia virus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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