3GWN

Crystal structure of the FAD binding domain from mimivirus sulfhydryl oxidase R596

3GWN の概要

• エントリーDOI: 10.2210/pdb3gwn/pdb
• 関連するPDBエントリー: 1JR8 1OQC 2HJ3 3GWL
• 分子名称: Probable FAD-linked sulfhydryl oxidase R596, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: five helix bundle, homodimer, disulfide bond, fad, flavoprotein, oxidoreductase, virion
• 由来する生物種: Acanthamoeba polyphaga mimivirus (APMV)
• 細胞内の位置: Virion : Q5UP54
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28545.47

構造登録者

Hakim, M.,Fass, D. (登録日: 2009-04-01, 公開日: 2009-07-07, 最終更新日: 2024-11-20)

主引用文献

Hakim, M.,Fass, D.
Dimer interface migration in a viral sulfhydryl oxidase
J.Mol.Biol., 391:758-768, 2009

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: 19576902
DOI: 10.1016/j.jmb.2009.06.070

実験手法

X-RAY DIFFRACTION (1.78 Å)