3qzy

Structure of Baculovirus Sulfhydryl Oxidase Ac92Structure of Baculovirus Sulfhydryl Oxidase Ac92

Structural highlights 3qzy is a 2 chain structure with sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FLSO_NPVAC Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV). Publication Abstract from PubMed Genomes of nucleocytoplasmic large DNA viruses (NCLDVs) encode enzymes that catalyze the formation of disulfide bonds between cysteine amino acid residues in proteins, a function essential for the proper assembly and propagation of NCLDV virions. Recently, a catalyst of disulfide formation was identified in baculoviruses, a group of large double-stranded DNA viruses considered phylogenetically distinct from NCLDVs. The NCLDV and baculovirus disulfide catalysts are flavin adenine dinucleotide (FAD)-binding sulfhydryl oxidases related to the cellular Erv enzyme family, but the baculovirus enzyme, the product of the Ac92 gene in Autographa californica multiple nucleopolyhedrovirus (AcMNPV), is highly divergent at the amino acid sequence level. The crystal structure of the Ac92 protein presented here shows a configuration of the active-site cysteine residues and bound cofactor similar to that observed in other Erv sulfhydryl oxidases. However, Ac92 has a complex quaternary structural arrangement not previously seen in cellular or viral enzymes of this family. This novel assembly comprises a dimer of pseudodimers with a striking 40-degree kink in the interface helix between subunits. The diversification of the Erv sulfhydryl oxidase enzymes in large double-stranded DNA viruses exemplifies the extreme degree to which these viruses can push the boundaries of protein family folds. Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the erv flavoenzyme family.,Hakim M, Mandelbaum A, Fass D J Virol. 2011 Sep;85(18):9406-13. Epub 2011 Jul 13. PMID:21752922 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfhydryl oxidase 3D structures

spinqualitylabelsall models 3qzy, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image