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1.8.4.12: peptide-methionine (R)-S-oxide reductase

This is an abbreviated version!
For detailed information about peptide-methionine (R)-S-oxide reductase, go to the full flat file.

Word Map on EC 1.8.4.12

Reaction

L-methionine (R)-sulfoxide
+
thioredoxin
=
L-methionine
+
thioredoxin disulfide
+
H2O

Synonyms

1-Cys methionine sulfoxide reductase B, 1-Cys MSRB, CBS-1, CBS1, cysteine-containing methionine-R-sulfoxide reductase, LOC100305558, LOC100798757, methionine sulfoxide reductase, methionine sulfoxide reductase B, methionine sulfoxide reductase B1, methionine sulfoxide reductase B2, methionine sulfoxide reductase B3, methionine sulfoxide reductase B8, methionine sulfoxide reductase MsrB3, methionine sulfoxide reductases B, methionine sulfoxide reductases B2, methionine sulphoxide reductase, methionine-R-sulfoxide reductase, methionine-R-sulfoxide reductase B, methionine-R-sulfoxide reductase B2, MetO reductase, More, MSR, MsrA, MsrA/B, MsrA/MsrB, msrAB, MsrABTk, MsrB, MSRB1, MsrB2, MsrB3, MsrB3A, MSRB4, MsrB5, MsrB7, MsrB8, MsrBA, Mxr2, NtMsrB2, OsMSRB5, PaMsrB1, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase type B, PilB, PilB protein, PMSR, Sel-X, selenocysteine-containing methionine-R-sulfoxide reductase, selenoprotein R, SelR, sulindac reductase, TbmsrB, TCDM_06423, YeaA

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.12 peptide-methionine (R)-S-oxide reductase

Crystallization

Crystallization on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapor-diffusion method. The crystals belong to the trigonal space group P3, with unit-cell parameters a = b = 136.096, c = 61.918 , and diffracted to 2.5 A resolution
-
sitting drop vapor diffusion method, crystal structure of HpMsrAB C44S/C318S at 2.2 A, which shows that a linker region (Hpiloop, 193-205) between two domains interacts with each HpMsrA or HpMsrB domain via three salt bridges (E193-K107, D197-R103, and K200-D339)
hanging drop vapor diffusion method, crystals diffracting to 1.87 A resolution, the MsrB3 structure is determined by using X-ray crystallography
purified recombinant detagged MsrB domain containing SeMet39, hanging drop vapour-diffusion method, 15 mg/ml protein in 20 mM Tris, pH 8.5, 10% v/v glycerol, against a well solution containing 0.1 M sodium cacodylate, pH 6.5, 30% w/v PEG 4000, room temperature, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
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
-
batch method, using 30% PEG 400, 0.1 M Tris-HCl (pH 8.5), and 0.2 M Na-citrate
selenomethionine-substituted peptide methionine sulfoxide reductase B domain, hanging drop vapour diffusion method in multiwell tissue-culture plates, 0.004 ml protein solution containing 75 mg/ml protein in 50 mM Tris-HCl, pH 8.0, mixed with 0.004 ml precipitant solution at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
to 2.3 A resolution, in presence and absence of dithiothreitol
batch method, crystals of the oxidized form are obtained by 32% PEG 4000, 0.8 M LiCl, and 0.1 M Tris HCl (pH 8.5), no crystal is obtained for wild type Xanthomonas campestris MsrB in its reduced form