Literature summary extracted from
Brot, N.; Collet, J.F.; Johnson, L.C.; Jonsson, T.J.; Weissbach, H.; Lowther, W.T.
The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases (2006), J. Biol. Chem., 281, 32668-32675.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.8.4.12 |
gene pilB, expression of N-terminally His-tagged full-length wild-type and mutant PilB and MsrB domain variants in Escherichia coli |
Neisseria gonorrhoeae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.8.4.12 |
purified recombinant PilB mutant L38M/L41M, vapour diffusion method, 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 100 mM NaCl, is mixed with well solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 26% PEG 2000 monomethylester, and 25% glycerol, X-ray diffraction structure determination and analysis at 1.6 A resolution, multiwavelength anomalous dispersion at -170°C |
Neisseria gonorrhoeae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.8.4.12 |
L38M/L41M |
site-directed mutagenesis, mutation of the NT domain of PilB, thioredoxin binding structure, crystal structure analysis, overview |
Neisseria gonorrhoeae |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.8.4.12 |
periplasm |
- |
Neisseria gonorrhoeae |
- |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.8.4.12 |
additional information |
PilB is a selenocysteine-containing enzyme |
Neisseria gonorrhoeae |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.8.4.12 |
additional information |
Neisseria gonorrhoeae |
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.8.4.12 |
Neisseria gonorrhoeae |
- |
bifunctional enzyme MsrA/B, gene pilB |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.8.4.12 |
recombinant N-terminally His-tagged full-length PilB and MsrB domain variants from Escherichia coli by nickel affinity chromatography followed by cleavage of the His-Tag through thrombin, followed by gel filtration and ion exchange chomatography |
Neisseria gonorrhoeae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.8.4.12 |
additional information |
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview |
Neisseria gonorrhoeae |
? |
- |
? |
|
1.8.4.12 |
additional information |
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview |
Neisseria gonorrhoeae |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.8.4.12 |
MsrB |
- |
Neisseria gonorrhoeae |
1.8.4.12 |
PilB |
- |
Neisseria gonorrhoeae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.8.4.12 |
37 |
- |
assay at |
Neisseria gonorrhoeae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.8.4.12 |
7.4 |
- |
assay at |
Neisseria gonorrhoeae |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.8.4.12 |
thioredoxin |
PilB contains an N-terminal thioredoxin-like domain, the NT domain, fused to the MsrA and MSrB domains, structure overview |
Neisseria gonorrhoeae |
|