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Default Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

Related Articles Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

J Biomol NMR. 2017 Nov 08;:

Authors: Wiegand T, Liao WC, Ong TC, Dšpp A, Cadalbert R, Copťret C, BŲckmann A, Meier BH

Abstract
DNP (dynamic nuclear polarization)-enhanced solid-state NMR is employed to directly detect protein-DNA and protein-ATP interactions and identify the residue type establishing the intermolecular contacts. While conventional solid-state NMR can detect protein-DNA interactions in large oligomeric protein assemblies in favorable cases, it typically suffers from low signal-to-noise ratios. We show here, for the oligomeric DnaB helicase from Helicobacter pylori complexed with ADP and single-stranded DNA, that this limitation can be overcome by using DNP-enhanced spectroscopy. Interactions are established by DNP-enhanced (31)P-(13)C polarization-transfer experiments followed by the recording of a 2D (13)C-(13)C correlation experiment. The NMR spectra were obtained in less than 2 days and allowed the identification of residues of the motor protein involved in nucleotide binding.


PMID: 29119516 [PubMed - as supplied by publisher]



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