Solid-state NMR 13C15N resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel

摘要

Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways. The regulatory aspect is conferred by a C-terminal cyclic nucleotide-binding domain (CNBD). We report resonance assignments of the CNBD of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magic-angle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a three-dimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances.Electronic supplementary materialThe online version of this article (doi:10.1007/s12104-012-9363-4) contains supplementary material, which is available to authorized users.