The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide . While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well . The enzyme from some species contains selenocysteine and Zn2+.
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.
the tandem domains of PilB also possess MsrA activity utilizing L-methionine (S)-sulfoxide as substrate, the MsrA domain alone does very poorly utilize the R-isomer
the tandem domains of PilB also possess MsrA activity utilizing L-methionine (S)-sulfoxide as substrate, the MsrA domain alone does very poorly utilize the R-isomer
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
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 separatly on the enzyme molecule, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
construction of truncated PilB domain forms, which show decreased survival of the organism to reactive oxygen species, the mutations do not affect piliation, pilin production, or adherence, overview
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
gene pilB, transposon insertion, truncated PilB enzyme forms of the enzyme lacking the MsrA domain from strain MS11, variant VD300, overexpression of the His-tagged PilB forms in Escherichia coli strain Xl-1 blue