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

Biomol NMR Assign. 2016 Apr;10(1):13-23. doi: 10.1007/s12104-015-9629-8. Epub 2015 Aug 18.

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.

Keywords: Assignments; HpDnaB; Secondary chemical shifts; Solid-state NMR; ssFLYA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • DnaB Helicases / chemistry*
  • Helicobacter pylori / enzymology*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Domains
  • Protein Structure, Secondary
  • Software

Substances

  • DnaB Helicases