KcsA - Prokaryotic pH-gated Potassium Channel
Family:
Prokaryotic Tetrameric Potassium Channels
Topology:
The channel protein contains two transmembrane helices (M1 and M2). The channel itself is a tetramer composed of four identical subunits so that the M2 helix faces the central pore, while the other M1 helix faces the lipid membrane.
History and function:
KcsA was the first potassium ion channel to be characterized using x-ray crystallography by Roderick MacKinnon and his colleagues in 1998. As one of the most studied ion channels to this day, KcsA is a template for research on K+ channel function. The KcsA channel is considered a model channel because its structure provides a framework for understanding K+ channel conduction, which has three parts: Potassium selectivity, channel gating by pH sensitivity, and voltage-gated channel inactivation.
Data and Applications
KcsA - Single Channel Recordings
Orbit 16 and applications:
Data were kindly provided by Ionera.
Single channel currents of tetrameric potassium channel KcsA E71A recorded from 5 selected bilayers in parallel.
KcsA was expressed in vitro with its co-translational integration into liposoms containing asolectin lipids. The proteoliposomes were subsecuently fused with bilayer array containing POPE/POPG on the Orbit 16.
Conditions: Current traces were recorded in 20 mM MES pH 4.0 on the cis-side and 10 mM MOPS, pH 7.0 on the trans-side of the bilayer; containing 200 mM KCl symmetric solutions with membrane potential held at +150 mV.
KcsA - Bilayer Recordings
Vesicle Prep Pro data and applicatons:
The image shows a representative current trace recorded from a planar lipid bilayer in which purified KcsA channels were reconstituted (100 mM KCl, asymmetric pH; pH 4/pH 7). A ramp from -100 mV to +100 mV was used to evoke the single channel events.
Download: Application Note
Application Notes
KcsA - "Lipid bilayer recordings of KcsA channels reconstituted in proteoliposomes"
Port-a-Patch and Vesicle Prep Pro application note: 
(0.2 MB)
Posters
2016 - Parallel and automated formation of lipid bilayers on microstructured chips for ion channel and nanopore recordings
Orbit 16 poster (1.4 MB)
Kindly provided by Ionera Technologies
Webinars
27.01.2016 | Webinar: Instant bilayers - just add protein.
Orbit 16 and 
Orbit Mini
This webinar covers the use of the lipid bilayer platforms from Nanion: the Orbit16 and the Orbit mini for characterization of membrane proteins like ion channels, bacterial porins and biological nanopores. Both bilayer systems support high quality low noise recordings, but differ in throughput capabilities and experimental features. The Orbit16, introduced in 2012 is a device for efficient formation of 16 lipid bilayers simultaneously, allowing for parallel bilayer-reconstitution of ion channels and nanopores.
Publications
2019 - Modulation of the potassium channel KcsA by anionic phospholipids: Role of arginines at the non-annular lipid binding sites
Port-a Patch Publication in BBA - Biomembranes (2019)
Authors:
Poveda J.A., Giudici A.M., Renart M.L., Millet O., Morales A., González-Ros J.M., Oakes V., Furini S., Domene C
2018 - Functional Analysis of Membrane Proteins Produced by Cell-Free Translation
Port-a-Patch and 
Orbit mini article in Protein Engineering (2018)
Authors:
Dondapati S.K., Wüstenhagen D.A., Kubick S.
2016 - Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola
Port-a-Patch and Vesicle Prep Pro publication in Nature Communications (2016)
Authors:
Dhakshnamoorthy B., Rohaim A., Rui H., Blachowicz L., Roux B.
2015 - Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration
Port-a-Patch and Vesicle Prep Pro publication in Journal of Biological Chemistry (2015)
Authors:
Carrara G., Saraiva N., Parsons M., Byrne B., Prole D.L., Taylor C.W., Smith G.L.
2014 - Membrane assembly of the functional KcsA potassium channel in a vesicle-based eukaryotic cell-free translation system
Port-a-Patch and Vesicle Prep Pro publication in Biosensors and Bioelectronics (2014)
Authors:
Dondapati S.K., Kreir M., Quast R.B., Wüstenhagen D.A., Brüggemann A., Fertig N., Kubick S.