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Literature summary for 1.8.3.2 extracted from

  • Hakim, M.; Fass, D.
    Dimer interface migration in a viral sulfhydryl oxidase (2009), J. Mol. Biol., 391, 758-768.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified unlabeled and selenomethionine-labeled pB119L-DELTAC, the protein crystallizes readily under a wide range of conditions, multiple anomalous dispersion, X-ray diffraction structure determination and analysis at 1.9 A resolution African swine fever virus

Protein Variants

Protein Variants Comment Organism
yes a truncated pB119L version lacking 16 residues at the carboxy terminus, i.e. pB119L-DELTAC, is a soluble protein African swine fever virus

Organism

Organism UniProt Comment Textmining
African swine fever virus Q65163
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
African swine fever virus

Purification (Commentary)

Purification (Comment) Organism
pB119L is located in the insoluble fraction, it can be solubilized by addition of arginine, and a truncated version lacking 16 residues at the carboxy terminus is a soluble protein African swine fever virus

Subunits

Subunits Comment Organism
dimer the viral enzyme uses an alternate dimerization mode compared to other viral sulfhydryl oxidases, overview. The dimer interface involves helices alpha2 and alpha3 African swine fever virus
More structure determination, comparison, and modelling, overview African swine fever virus

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the sulfhydryl oxidases of the Erv/ALR family African swine fever virus
pB119L
-
African swine fever virus
sulfhydryl oxidase
-
African swine fever virus

Cofactor

Cofactor Comment Organism Structure
FAD flavoenzyme African swine fever virus