1.8.4.11: peptide-methionine (S)-S-oxide reductase

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

Reaction

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

Synonyms

ecdysone-induced protein 28/29 kDa, FMsr, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MSRA2, MSRA4, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase

ECTree

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

Crystallization

Crystallization on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1-Cys type selenoprotein MsrA at 1.61.8 A, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure folds into a catalytic domain and a helical domain absent from other known MsrA structures. The side chain length of residue Glu55 is critical for its proton donor function
-
structure of dimeric MsrA to 2.9 A resolution, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole
-
molecular modeling. The conserved residue Glu99 is buried in the Met-S-(O) groove, which might contribute to the correct placing of substrates. Residue Asp134 does not form hydrogen bonds with the substrates but only within the enzyme
-
15-50 mg/ml purified recombinant MsrA in 50 mM Tris-HCl, pH 8.0, 2 mM EDTA, and 10 mM DTT, hanging drop vapour diffusion method, droplet size is 0.004-0.008 ml, equal volumes of protein and precipitant solution, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
single crystals of recombinant N-terminally 10His-tagged enzyme MsrA complexed with protein-bound methionine, hanging drop method, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 1 mM EDTA, 1 mM tris(carboxyethyl)phosphine hydrochloride, precipitant solution contains 2.0 M sodium formate, 0.1 M sodium citrate, pH 6.0, 4C, 1 week, prior to data collection, crystals are soaked in 6.3 M sodium formate, 0.1 M sodium citrate, pH 6.0, for 2 min, and are flash-cooled, X-ray diffraction structure determination and analysis at 1.5 A resolution, polycrystalline clusters are obtained by sitting drop vapor diffusion method
-
crystals are obtained using the microbatch-under-oil method, four structures of the MsrA domain of the PilB protein from Neisseria meningitidis, representative of four catalytic intermediates of the MsrA catalytic cycle, are determined by X-ray crystallography
-
three-dimensional structure of MsrA in complex with AcMetSONHMe obtained by X-ray crystallography
-
to 2.3 A resolution, in presence and absence of dithiothreitol