3GWL
Crystal structure of ASFV pB119L, a viral sulfhydryl oxidase
Summary for 3GWL
| Entry DOI | 10.2210/pdb3gwl/pdb |
| Related | 1JR8 1OQC 2HJ3 3GWN |
| Descriptor | FAD-linked sulfhydryl oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | homodimer, five-helix bundle, disulfide bond, fad, flavoprotein, late protein, oxidoreductase, virulence |
| Biological source | African swine fever virus BA71V (ASFV) |
| Cellular location | Host cytoplasm : Q65163 |
| Total number of polymer chains | 2 |
| Total formula weight | 27384.31 |
| Authors | |
| Primary citation | Hakim, M.,Fass, D. Dimer interface migration in a viral sulfhydryl oxidase J.Mol.Biol., 391:758-768, 2009 Cited by PubMed Abstract: Large double-stranded DNA viruses, including poxviruses and mimiviruses, encode enzymes to catalyze the formation of disulfide bonds in viral proteins produced in the cell cytosol, an atypical location for oxidative protein folding. These viral disulfide catalysts belong to a family of sulfhydryl oxidases that are dimers of a small five-helix fold containing a Cys-X-X-Cys motif juxtaposed to a flavin adenine dinucleotide cofactor. We report that the sulfhydryl oxidase pB119L from African swine fever virus (ASFV) uses for self-assembly surface different from that observed in homologs from mammals, plants, and fungi. Within a protein family, different packing interfaces for the same oligomerization state are extremely rare. We find that the alternate dimerization mode seen in ASFV pB119L is not characteristic of all viral sulfhydryl oxidases, as the flavin-binding domain from a mimivirus sulfhydryl oxidase assumes the same dimer structure as the known eukaryotic enzymes. ASFV pB119L demonstrates the potential of large double-stranded DNA viruses, which have faster mutation rates than their hosts and the tendency to incorporate host genes, to pioneer new protein folds and self-assembly modes. PubMed: 19576902DOI: 10.1016/j.jmb.2009.06.070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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