NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus.
Isotopically labeled, 15N and 15N/13C forms of recombinant methionine-r-sulfoxide reductase 1 (MsrB1, SelR) from Mus musculus were produced, in which catalytic selenocysteine was replaced with cysteine. We report here the 1H, 13C and 15N NMR assignment of the reduced form of this mammalian protein.
Sal
Lena S
LS
Department of Biotechnology, Norwegian University of Science and Technology, Sem Saelands vei 6/8, Trondheim 7491, Norway.
Aachmann
Finn L
FL
Kim
Hwa-Young
HY
Gladyshev
Vadim N
VN
Dikiy
Alexander
A
D019943:Amino Acid Substitution; D000818:Animals; D020134:Catalytic Domain / Q000235:genetics; D051150:Methionine Sulfoxide Reductases; D051379:Mice; D008840:Microfilament Proteins; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D008840:Microfilament Proteins; D011994:Recombinant Proteins; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C520510:Msrb2 protein, mouse