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x * 47000, SDS-PAGE
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x * 22000, full length enzyme, SDS-PAGE
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x * 45000, SDS-PAGE, x * 43959, mass spectrometry
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x * 45000, SDS-PAGE, x * 43959, mass spectrometry
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x * 90000, may exist in an aggregated molecular form, SDS-PAGE
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x * 68000, recombinant His-tagged enzyme, SDS-PAGE
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x * 100000, native enzyme, SDS-PAGE
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x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
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x * 65000, recombinant enzyme, SDS-PAGE
dimer
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2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
the viral enzyme uses an alternate dimerization mode compared to other viral sulfhydryl oxidases, overview. The dimer interface involves helices alpha2 and alpha3
dimer
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2 * 14378, laser desorption mass spectrometry
dimer
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1 * 50000 plus 1 * 55000, SDS-PAGE
dimer
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1 * 50000 plus 1 * 55000, SDS-PAGE
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dimer
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
dimer
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2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
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dimer
2 * 33000, calculated and crystallization data
dimer
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2 * 93000, SDS-PAGE
dimer
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monomers are linked via a disulfide bridge C15-C124, which is not critical for dimer formation, structure modeling using the enzymes crystal structure
dimer
crystal structure, stabilization by extensive noncovalent interactions and a network of hydrogen bonds, structure fo the dimer interface
dimer
1 * 23000, 1* 21000, SDS-PAGE, under non-reducing conditions
dimer
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2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
dimer
Cys30 and Cys33 are involved in dimer formation
dimer
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2 * 70000, also aggregates to larger multimers, SDS-PAGE
homodimer
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monomer
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1 * 14000, SDS-PAGE, in the infected cell
monomer
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1 * 66000, SDS-PAGE
monomer
1 * 21000, SDS-PAGE, under reducing conditions
monomer
1 * 23000, SDS-PAGE, under reducing conditions
monomer
1 * 54000, SDS-PAGE
additional information
structure determination, comparison, and modelling, overview
additional information
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structure determination, comparison, and modelling, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
structural analysis, modeling of the conserved central domain, the plant enzyme contains a unique C-terminally located CXXXXC motif and no N-terminally localized cysteine pair, which is typical for enzymes of the Erv1/Alr sulfhydryl oxidase family
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
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additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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structure
additional information
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2 enzyme fragments by partial proteolysis: a 30 kDa nonglycosylated monomeric fragment containing a thioredoxin domain with a CXXC motif, and a 60 kDa glycosylated dimeric fragment with bound FAD and catalytic activity, the latter different from intact enzyme activity
additional information
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enzyme contains an N-terminal thioredoxin domain, an intervening domain, and a C-terminal ALR/ERV domain, redox-active motif CXXC
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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isozyme domain structure, overview
additional information
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isozyme domain structure, two splicing variants, overview
additional information
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
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enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
structural analysis of the recombinant enzyme
additional information
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structural analysis of the recombinant enzyme
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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structure, active site structure containinbg a CXXC motif
additional information
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Erv1p contains three conserved disulfide bonds arranged in two CXXC motifs and one CX16C motif in the highly conserved central catalytic core. The CX16C disulfide plays an important role in stabilizing the folding of Erv1p, both CXXC disulfides are required for Erv1 oxidase activity, but none of the disulfide is essential for FAD binding, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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domain organization of TbQSOX together with key catalytic steps deduced from studies of both metazoan and protist QSOXs, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview