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Literature summary for 1.7.2.3 extracted from

  • Tranier, S.; Mortier-Barriere, I.; Ilbert, M.; Birck, C.; Iobbi-Nivol, C.; Mejean, V.; Samama, J.P.
    Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA (2002), Protein Sci., 11, 2148-2157.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene torD, DNA sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) as His-tagged protein Shewanella massilia

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant monomeric, dimeric, and trimeric forms, hanging drop vapour diffusion method, 4°C, 0.001 ml of 1.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, 10 mM DTT, mixed with equal volume of reservoir solution containing 1.6 M ammonium sulfate, 100 mM MES, pH 6.4, 4-6 days, cryoprotection by addition of 15% w/v ethylene glycerol to the reservoir solution, X-ray diffraction structure determination and analysis at 2.42 A resolution Shewanella massilia

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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Shewanella massilia 5737
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19500
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
24100
-
monomeric form, small-angle X-ray scattering Shewanella massilia
24350 24360 monomeric form, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
24356
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
25000
-
1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
27900
-
2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
47800
-
dimeric form, small-angle X-ray scattering Shewanella massilia
48710
-
dimeric form, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Shewanella massilia enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently ?
-
?

Organism

Organism UniProt Comment Textmining
Shewanella massilia
-
TorD, cytoplasmic chaperone of trimethylamine reductase TorA, EC 1.6.6.9, encoded in the tor operon together with TorA and a pentahemic c-type cytochrome
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged monomeric, dimeric, and trimeric forms from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography, and gel filtration for the the monomeric form Shewanella massilia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently Shewanella massilia ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 24356, sedimentation equilibrium analysis, 2 * 27900, dimeric form, Guinier analysis Shewanella massilia
monomer 1 * 24100, monomeric form, small-angle X-ray scattering, 1 * 19500, monomeric form, Guinier analysis, 1 * 25000, monomeric form, non-denaturing PAGE, 1 * 24354-24356, mass spectrometry and sedimentation equilibrium analysis Shewanella massilia
More enzyme forms multiple and stable oligomeric species, e.g. monomers, dimers, and trimers, analysis by ultracentrifugation, small-angle X-ray scattering, preliminary diffraction, and circular dichroism spectra, interconversion of the native oligomeric forms at pH 3.0 Shewanella massilia

Synonyms

Synonyms Comment Organism
TorD
-
Shewanella massilia

Cofactor

Cofactor Comment Organism Structure
cytochrome c pentahemic Shewanella massilia