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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

Author

Listed:
  • Federica Castellani

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

  • Barth van Rossum

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

  • Annette Diehl

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

  • Mario Schubert

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

  • Kristina Rehbein

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

  • Hartmut Oschkinat

    (Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin)

Abstract

The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not accessible to solution NMR, such as amyloid systems1 or membrane proteins2,3,4. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete 13C and 15N resonance assignments for a micro-crystalline preparation of the α-spectrin Src-homology 3 (SH3) domain5 formed the basis for the extraction of a set of distance restraints. These restraints were derived from proton-driven spin diffusion (PDSD) spectra of biosynthetically site-directed, labelled samples obtained from bacteria grown using [1,3-13C]glycerol or [2-13C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to ∼7 Å. The calculated global fold of the α-spectrin SH3 domain is based on 286 inter-residue 13C–13C and six 15N–15N restraints, all self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure should be widely applicable to small membrane proteins that can be expressed in bacteria.

Suggested Citation

  • Federica Castellani & Barth van Rossum & Annette Diehl & Mario Schubert & Kristina Rehbein & Hartmut Oschkinat, 2002. "Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy," Nature, Nature, vol. 420(6911), pages 99-102, November.
  • Handle: RePEc:nat:nature:v:420:y:2002:i:6911:d:10.1038_nature01070
    DOI: 10.1038/nature01070
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    1. Jianping Li & Ampon Sae Her & Alida Besch & Belen Ramirez-Cordero & Maureen Crames & James R. Banigan & Casey Mueller & William M. Marsiglia & Yingkai Zhang & Nathaniel J. Traaseth, 2024. "Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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