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NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus

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Abstract

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, 15N and 13C NMR assignment of the reduced form of this mammalian protein.

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Acknowledgments

This research was supported by the Faculty of Natural Sciences and Technology (NT faculty) of the Norwegian University of Science and Technology (NTNU), NIH AG021518 and KOSEF R13-2005-005-01004-0. The 800 MHz NMR spectra for assignment of aromatic residues of MsrB1 protein were recorded with a cryoprobe at the NMR center at the University of Florence within the EUNMR project (Contract # RII3-026145).

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Authors and Affiliations

  1. Department of Biotechnology, Norwegian University of Science and Technology, Sem Sælands vei 6/8, Trondheim, 7491, Norway

    Lena S. Sal, Finn L. Aachmann & Alexander Dikiy

  2. Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu, 705-717, South Korea

    Hwa-Young Kim

  3. Department of Biochemistry, University of Nebraska, Lincoln, NE, 68588, USA

    Vadim N. Gladyshev

Authors
  1. Lena S. Sal
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  2. Finn L. Aachmann
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  3. Hwa-Young Kim
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  4. Vadim N. Gladyshev
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  5. Alexander Dikiy
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Correspondence to Alexander Dikiy.

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Sal, L.S., Aachmann, F.L., Kim, HY. et al. NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus . Biomol NMR Assign 1, 131–133 (2007). https://doi.org/10.1007/s12104-007-9039-7

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  • DOI: https://doi.org/10.1007/s12104-007-9039-7

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