Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel.
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.
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Abhishek
A
Cukkemane
Deepak
D
Nand
Sabine
S
Gradmann
Markus
M
Weingarth
U Benjamin
UB
Kaupp
Marc
M
Baldus
D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D054815:Cyclic Nucleotide-Gated Cation Channels / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D009711:Nucleotides / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D054815:Cyclic Nucleotide-Gated Cation Channels; D009587:Nitrogen Isotopes; D009711:Nucleotides