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- Title
Mapping the structure and conformational movements of proteins with transition metal ion FRET.
- Authors
Taraska, Justin W; Puljung, Michael C; Olivier, Nelson B; Flynn, Galen E; Zagotta, William N
- 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.
- Publication
Nature methods, 2009, Vol 6, Issue 7, p532
- ISSN
1548-7105
- Publication type
Journal Article
- DOI
10.1038/nmeth.1341