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Literature summary for 1.8.5.9 extracted from

  • Christensen, S.; Halili, M.; Strange, N.; Petit, G.; Huston, W.; Martin, J.; McMahon, R.
    Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development (2019), PLoS ONE, 14, e0222595 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.5.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C41(DE3) cells Chlamydia trachomatis
gene dsbB, recombinant expression of recombinant enzyme in Escherichia coli, coexpression with Chlamydia trachomatis dsbA Chlamydia trachomatis

Protein Variants

Protein Variants Comment Organism
additional information construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA Chlamydia trachomatis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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 Chlamydia trachomatis 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[DsbA protein] with reduced L-cysteine residues + quinone Chlamydia trachomatis overall reaction [DsbA protein] carrying a disulfide bond + quinol
-
 ?
[DsbA protein] with reduced L-cysteine residues + quinone Chlamydia trachomatis A2497 overall reaction [DsbA protein] carrying a disulfide bond + quinol
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis
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-
-
Chlamydia trachomatis G4NNC5 serovar A
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Chlamydia trachomatis A2497 G4NNC5 serovar A
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Purification (Commentary)

Purification (Comment) Organism
His-Trap column chromatography and Superdex 200 gel filtration Chlamydia trachomatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation Chlamydia trachomatis ?
-
-
additional information membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation Chlamydia trachomatis A2497 ?
-
-
[DsbA protein] with reduced L-cysteine residues + quinone overall reaction Chlamydia trachomatis [DsbA protein] carrying a disulfide bond + quinol
-
 ?
[DsbA protein] with reduced L-cysteine residues + quinone overall reaction Chlamydia trachomatis A2497 [DsbA protein] carrying a disulfide bond + quinol
-
 ?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1 overall reaction Chlamydia trachomatis [DsbA protein] carrying a disulfide bond + ubiquinol-1
-
 ?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1 overall reaction Chlamydia trachomatis A2497 [DsbA protein] carrying a disulfide bond + ubiquinol-1
-
 ?

Synonyms

Synonyms Comment Organism
C. trachomatis disulfide bond protein B
-
 Chlamydia trachomatis
CtDsbB
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 Chlamydia trachomatis
disulfide bond protein B
-
 Chlamydia trachomatis
DsbB
-
 Chlamydia trachomatis

Expression

Organism Comment Expression
Chlamydia trachomatis CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds up

General Information

General Information Comment Organism
physiological function disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB Chlamydia trachomatis