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

Federica Castellani, Barth van Rossum (), Annette Diehl, Mario Schubert, Kristina Rehbein and Hartmut Oschkinat ()
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Federica Castellani: Forschungsinstitut für Molekulare Pharmakologie
Barth van Rossum: Forschungsinstitut für Molekulare Pharmakologie
Annette Diehl: Forschungsinstitut für Molekulare Pharmakologie
Mario Schubert: Forschungsinstitut für Molekulare Pharmakologie
Kristina Rehbein: Forschungsinstitut für Molekulare Pharmakologie
Hartmut Oschkinat: Forschungsinstitut für Molekulare Pharmakologie

Nature, 2002, vol. 420, issue 6911, 99-102

Abstract: 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.

Date: 2002
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DOI: 10.1038/nature01070

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