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TitleLigand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.
Journal, issue, pagesNat Commun, Vol. 5, Page 3106, Year 2014
Publish dateOct 27, 2015
AuthorsJulia Kowal / Mohamed Chami / Paul Baumgartner / Marcel Arheit / Po-Lin Chiu / Martina Rangl / Simon Scheuring / Gunnar F Schröder / Crina M Nimigean / Henning Stahlberg /
PubMed AbstractCyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly ...Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels.
External linksNat Commun / PubMed:24469021 / PubMed Central
MethodsEM (electron crystallography)
Resolution7.0 Å
Structure data

2526

4chv

EMDB-2526, PDB-4chv:
The electron crystallography structure of the cAMP-bound potassium channel MloK1
Method: EM (electron crystallography) / Resolution: 7.0 Å

2527

4chw

EMDB-2527, PDB-4chw:
The electron crystallography structure of the cAMP-free potassium channel MloK1
Method: EM (electron crystallography) / Resolution: 7.0 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • mesorhizobium loti (bacteria)
KeywordsTRANSPORT / 2DX / VOLTAGE GATED POTASSIUM CHANNEL / CNBD / 2D CRYSTAL / TRANSPORT PROTEIN

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