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Literature summary for 1.8.4.16 extracted from

  • Smith, R.; Mohanty, B.; Williams, M.; Scanlon, M.; Heras, B.
    HN, N, Calpha and Cbeta assignments of the two periplasmic domains of Neisseria meningitidis DsbD (2017), Biomol. NMR Assign., 11, 181-186 .
    View publication on PubMed
Search for more literature for 1.8.4.16

Cloned(Commentary)

Cloned (Comment) Organism
gene dsbD, recombinant individual expression of the C- and N-terminal domains of the enzyme with an N-terminal His6-tag followed by a tobacco etch virus (TEV) protease cleavage site in Escherichia coli strain BL21(DE3) pLysS Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
C103S site-directed mutagenesis Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Neisseria meningitidis 5737
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additional information two periplasmic domains of native NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms Neisseria meningitidis
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Organism

Organism UniProt Comment Textmining
Neisseria meningitidis Q9JYM0
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Neisseria meningitidis NMB Q9JYM0
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme domains by nickel affinity chromatography and gel filtration Neisseria meningitidis

Subunits

Subunits Comment Organism
More DsbD is an integral membrane protein comprising two periplasmic domains, n-DsbD and c-DsbD, which flank a transmembrane region, t-DsbD. Two periplasmic domains of native cytoplasmic NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms, structure analysis by NMR spectroscopy Neisseria meningitidis

Synonyms

Synonyms Comment Organism
disulfide bond reductase
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 Neisseria meningitidis
DsbD
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 Neisseria meningitidis
NmDsbD
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 Neisseria meningitidis

Cofactor

Cofactor Comment Organism Structure
thioredoxin
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 Neisseria meningitidis

General Information

General Information Comment Organism
additional information 13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview Neisseria meningitidis
physiological function NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation Neisseria meningitidis