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Default Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion

Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion


Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the assignment of this largest protein assigned today by solid-state NMR, and for which no solution-state NMR shifts were available. A comparison of the NMR chemical shifts with crystallographic data reveals that regions with high crystallographic B-factors are particularly difficult to assign. While the secondary structure elements derived from the chemical shift data correspond mainly to those present in the X-ray crystal structure, we detect an additional helical element and structural variability in the protein crystal, most probably originating from the different molecules in the asymmetric unit, with the observation of doubled resonances in several parts, including entire stretches, of the protein. Our results provide the point of departure towards an atomic-resolution structural analysis of the C-terminal Ure2p domain in the context of the full-length prion fibrils.
  • Content Type Journal Article
  • Pages 1-9
  • DOI 10.1007/s10858-011-9530-4
  • Authors
    • Birgit Habenstein, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon, France
    • Christian Wasmer, Harvard Medical School, Boston, MA 02115, USA
    • Luc Bousset, Laboratoire d??Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France
    • Yannick Sourigues, Laboratoire d??Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France
    • Anne Schütz, Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland
    • Antoine Loquet, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon, France
    • Beat H. Meier, Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland
    • Ronald Melki, Laboratoire d??Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France
    • Anja Böckmann, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367 Lyon, France

Source: Journal of Biomolecular NMR
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