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Solid-state NMR sequential assignments of the N-terminal domain of HpDnaB helicase

Authors :
Anja Böckmann
Denis Lacabanne
Thomas Wiegand
Britta Kunert
Laurent Terradot
Alexandre Bazin
Carole Gardiennet
Francesco Ravotti
Peter Güntert
Beat H. Meier
Riccardo Cadalbert
Physical Chemistry [ETH Zürich]
Department of Chemistry and Applied Biosciences [ETH Zürich] (D-CHAB)
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)- Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)
Cristallographie, Résonance Magnétique et Modélisations (CRM2)
Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)
Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB)
Université Claude Bernard Lyon 1 (UCBL)
Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)
Laboratorium für Physikalische Chemie (ETH-LPC)
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)
Institut de biologie et chimie des protéines [Lyon] (IBCP)
Institute of Biophysical Chemistry and Frankfurt Institute for Advanced Studies
Goethe-University Frankfurt am Main
Laboratory of Physical Chemistry [ETH Zürich] (LPC)
Source :
Biomolecular NMR Assignments, Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.13-23. ⟨10.1007/s12104-015-9629-8⟩, Biomolecular NMR Assignments, 10 (1)
Publication Year :
2016
Publisher :
HAL CCSD, 2016.

Abstract

We present solid-state NMR assignments of the N-terminal domain of the DnaB helicase from Helicobacter pylori (153 residues) in its microcrystalline form. We use a sequential resonance assignment strategy based on three-dimensional NMR experiments. The resonance assignments obtained are compared with automated resonance assignments computed with the ssFLYA algorithm. An analysis of the (13)C secondary chemical shifts determines the position of the secondary structure elements in this α-helical protein.

Details

Language :
English
ISSN :
1874270X
Database :
OpenAIRE
Journal :
Biomolecular NMR Assignments, Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.13-23. ⟨10.1007/s12104-015-9629-8⟩, Biomolecular NMR Assignments, 10 (1)
Accession number :
edsair.doi.dedup.....afa871e7ab9ab061d5f2788382877a61
Full Text :
https://doi.org/10.1007/s12104-015-9629-8⟩