3ETQ

X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids 443-630 including C508N, C584S, and C601S mutations

Summary for 3ETQ

• Entry DOI: 10.2210/pdb3etq/pdb
• Related: 1Q3E 1Q43 1Q5O 2Q0A 3BPZ
• Descriptor: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: hcn, ion channel, camp, cyclic nucleotide binding domain, beta roll, c-linker, camp-binding, glycoprotein, ion transport, ionic channel, membrane, nucleotide-binding, phosphoprotein, potassium, potassium channel, potassium transport, sodium, sodium channel, sodium transport, transmembrane, transport, voltage-gated channel, transport protein
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane ; Multi-pass membrane protein : O88703
• Total number of polymer chains: 2
• Total formula weight: 48400.88

Authors

Flynn, G.E. (deposition date: 2008-10-08, release date: 2009-06-23, Last modification date: 2023-09-06)

Primary citation

Taraska, J.W.,Puljung, M.C.,Olivier, N.B.,Flynn, G.E.,Zagotta, W.N.
Mapping the structure and conformational movements of proteins with transition metal ion FRET.
Nat.Methods, 6:532-537, 2009

PubMed Abstract: Visualizing conformational dynamics in proteins has been difficult, and the atomic-scale motions responsible for the behavior of most allosteric proteins are unknown. Here we report that fluorescence resonance energy transfer (FRET) between a small fluorescent dye and a nickel ion bound to a dihistidine motif can be used to monitor small structural rearrangements in proteins. This method provides several key advantages over classical FRET, including the ability to measure the dynamics of close-range interactions, the use of small probes with short linkers, a low orientation dependence, and the ability to add and remove unique tunable acceptors. We used this 'transition metal ion FRET' approach along with X-ray crystallography to determine the structural changes of the gating ring of the mouse hyperpolarization-activated cyclic nucleotide-regulated ion channel HCN2. Our results suggest a general model for the conformational switch in the cyclic nucleotide-binding site of cyclic nucleotide-regulated ion channels.

PubMed: 19525958
DOI: 10.1038/nmeth.1341

Experimental method

X-RAY DIFFRACTION (1.9 Å)