3FFQ

HCN2I 443-640 apo-state

Summary for 3FFQ

• Entry DOI: 10.2210/pdb3ffq/pdb
• Related: 1Q3E 1Q43 1Q5O 3BPZ
• Descriptor: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2, BROMIDE ION (3 entities in total)
• Functional Keywords: ion transport, ion channel, membrane, nucleotide-binding, potassium, potassium channel, sodium channel, transmembrane, voltage-gated channel, camp, camp-binding, glycoprotein, ionic channel, phosphoprotein, potassium transport, sodium transport, transport, metal transport
• Biological source: Mus musculus (mouse)
• Cellular location: Membrane; Multi-pass membrane protein: O88703
• Total number of polymer chains: 2
• Total formula weight: 47975.30

Authors

Olivier, N.B. (deposition date: 2008-12-04, 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 (2.4 Å)