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Literature summary for 5.3.4.1 extracted from

  • Heras, B.; Edeling, M.A.; Schirra, H.J.; Raina, S.; Martin, J.L.
    Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide (2004), Proc. Natl. Acad. Sci. USA, 101, 8876-8881.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified native and selenomethionine-labeled DsbG in oxidized and in redox-mixed state, DsbG is oxidized by 1.7 mM (1,10-phenanthroline)Cu(II), crystallization in 20% PEG 4000, 0.1 M sodium citrate, pH 3.8-4.2, and 0.2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
catalyses the rearrangement of -S-S- bonds in proteins the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert, and an active site motif -C-X-X-C-, active site structure Escherichia coli

Subunits

Subunits Comment Organism
dimer DsbG is a homodimer with an N-terminal dimerization domain on each subunit, crystal structure Escherichia coli
More the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert Escherichia coli

Synonyms

Synonyms Comment Organism
disulfide isomerase
-
Escherichia coli
DsbG
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Escherichia coli