Literature summary for 1.8.4.16 extracted from

Smith, R.; Whitten, A.; Paxman, J.; Kahler, C.; Scanlon, M.; Heras, B.
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis (2018), Acta Crystallogr. Sect. F, 74, 31-38 .

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21 (DE3) pLysS cells	Neisseria meningitidis

Crystallization (Commentary)

Crystallization (Comment)	Organism
periplasmic domains n-DsbD and c-DsbD in both redox states, hanging drop vapor diffusion method, using 18-20% (w/v) PEG 6000, 0.1 M MES pH 6.4, 0.02 M ZnCl2 (for the oxidized state of n-DsbD), 2.5 M ammonium sulfate, 0.1 M Tris pH 9.1 (for the reduced state of n-DsbD), 5% (w/v) PEG 400, 1.7-2.2 M citrate/citric acid pH 7.0-7.8 (for the oxidized state of c-DsbD), or 0.2 M zinc acetate dihydrate, 0.1 M sodium cacodylate trihydrate pH 7.5, 18% (w/v) PEG 8000 (for the reduced state of c-DsbD)	Neisseria meningitidis

Crystallization (Comment)

Organism

periplasmic domains n-DsbD and c-DsbD in both redox states, hanging drop vapor diffusion method, using 18-20% (w/v) PEG 6000, 0.1 M MES pH 6.4, 0.02 M ZnCl2 (for the oxidized state of n-DsbD), 2.5 M ammonium sulfate, 0.1 M Tris pH 9.1 (for the reduced state of n-DsbD), 5% (w/v) PEG 400, 1.7-2.2 M citrate/citric acid pH 7.0-7.8 (for the oxidized state of c-DsbD), or 0.2 M zinc acetate dihydrate, 0.1 M sodium cacodylate trihydrate pH 7.5, 18% (w/v) PEG 8000 (for the reduced state of c-DsbD)

Neisseria meningitidis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Neisseria meningitidis	16020	-

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
HisTrap column chromatography and Superdex S-75 gel filtration	Neisseria meningitidis

Synonyms

Synonyms	Comment	Organism
DsbD	-	Neisseria meningitidis

General Information

General Information	Comment	Organism
metabolism	the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence	Neisseria meningitidis
physiological function	the enzyme is required for the survival Neisseria meningitides	Neisseria meningitidis