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heterodimer
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1 * 23000 + 1 * 16000, SDS-PAGE
homodimer
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2 * 16000, SDS-PAGE
?
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x * 25000, MsrA
?
x * 29700, recombinant MsrA, SDS-PAGE
?
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x * 43000, Msr, SDS-PAGE
?
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x * 23649, calculated from amino acid sequence
?
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x * 21000-27000, about, recombinant MsrA, SDS-PAGE
?
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x * 21898, about, recombinant MsrA domain, mass spectrometry
?
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x * 20900, calculated from amino acid sequence
dimer
and monomer. Monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin
dimer
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and monomer. Monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin
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monomer
and dimer. monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin
monomer
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and dimer. monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin
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monomer
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1 * 20000, deduced from amino acid sequence
monomer
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1 * 20000, deduced from amino acid sequence
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additional information
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amino acid sequence comparison, structure analysis, active enzyme possesses no N-terminal coil before the core
additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
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the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity
additional information
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amino acid sequence comparison
additional information
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residual dipolar coupling determination and analysis, comparison with the crystal structure, protein fold and tertiary structure determination
additional information
amino acid sequence comparison, analysis of three-dimensional structures, N-terminal coil, structure comparison to enzymes from other species
additional information
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the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity
additional information
residual dipolar coupling determination and analysis, comparison with the crystal structure, protein fold and tertiary structure determination
additional information
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MsrA and MsrB, EC 1.8.4.12, are fused together
additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
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amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
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additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
enzyme domain and active site structure, MsrA domain comprises residues 181-362, overview
additional information
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the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
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amino acid sequence comparison
additional information
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MsrA activity is located on the central domain of PILB, the fused domains are folded entities
additional information
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MsrA and enzyme MsrB, methionine S-oxide reductase (R-form oxidizing), form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
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the enzyme forms are produced as individual folded entities, but in vivo the enzyme is part of a three-domain protein named PILB, with the central domain exhibiting MsrA activity, and the C-terminal domain showing MsrB activity
additional information
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solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
additional information
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amino acid sequence comparison