1M8M
SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN
Summary for 1M8M
| Entry DOI | 10.2210/pdb1m8m/pdb |
| Descriptor | SPECTRIN ALPHA CHAIN, BRAIN (1 entity in total) |
| Functional Keywords | solid-state mas nmr structure, structural protein |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cytoplasm, cytoskeleton: P07751 |
| Total number of polymer chains | 1 |
| Total formula weight | 7229.24 |
| Authors | Castellani, F.,Van Rossum, B.,Diehl, A.,Schubert, M.,Rehbein, K.,Oschkinat, H. (deposition date: 2002-07-25, release date: 2002-11-20, Last modification date: 2024-05-22) |
| Primary citation | Castellani, F.,Van Rossum, B.,Diehl, A.,Schubert, M.,Rehbein, K.,Oschkinat, H. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy Nature, 420:98-102, 2002 Cited by PubMed 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 systems or membrane proteins. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and (15)N resonance assignments for a micro-crystalline preparation of the alpha-spectrin Src-homology 3 (SH3) domain 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-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to approximately 7 A. The calculated global fold of the alpha-spectrin SH3 domain is based on 286 inter-residue (13)C-(13)C and six (15)N-(15)N 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. PubMed: 12422222DOI: 10.1038/nature01070 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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