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TitleHigh-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.
Journal, issue, pagesStructure, Vol. 26, Issue 1, Page 20-27.e3, Year 2018
Publish dateJan 2, 2018
AuthorsJulia Kowal / Nikhil Biyani / Mohamed Chami / Sebastian Scherer / Andrzej J Rzepiela / Paul Baumgartner / Vikrant Upadhyay / Crina M Nimigean / Henning Stahlberg /
PubMed AbstractEukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a ...Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium channel homolog from Mesorhizobium loti, MloK1, determined from 2D crystals in the presence of lipids. Even though crystals diffract electrons to only ∼10 Å, using cryoelectron microscopy (cryo-EM) and recently developed computational methods, we have determined a 3D map of full-length MloK1 in the presence of cyclic AMP (cAMP) at ∼4.5 Å isotropic 3D resolution. The structure provides a clear picture of the arrangement of the cyclic nucleotide-binding domains with respect to both the pore and the putative voltage sensor domains when cAMP is bound, and reveals a potential gating mechanism in the context of the lipid-embedded channel.
External linksStructure / PubMed:29249605
MethodsEM (electron crystallography)
Resolution4.5 Å
Structure data

3907

6eo1

EMDB-3907, PDB-6eo1:
The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)
Method: EM (electron crystallography) / Resolution: 4.5 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • Mesorhizobium loti (bacteria)
  • mesorhizobium loti maff303099 (bacteria)
KeywordsMEMBRANE PROTEIN / MloK1 / MlotiK1 / potassium channel / CNBD / cytoplasmic domains / PCO refinement

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