NDLI: Crystal structure of a Kir3.1-prokaryotic Kir channel chimera

Content Provider	PubMed Central
Author	Nishida, Motohiko Martine, Cadene Chait, Brian T. Mackinnon, Roderick
Copyright Year	2007
Abstract	The Kir3.1 K+ channel participates in heart rate control and neuronal excitability through G-protein and lipid signaling pathways. Expression in Escherichia coli has been achieved by replacing three fourths of the transmembrane pore with the pore of a prokaryotic Kir channel, leaving the cytoplasmic pore and membrane interfacial regions of Kir3.1 origin. Two structures were determined at 2.2 Å. The selectivity filter is identical to the Streptomyces lividans K+ channel within error of measurement (r.m.s.d.<0.2 Å), suggesting that K+ selectivity requires extreme conservation of three-dimensional structure. Multiple K+ ions reside within the pore and help to explain voltage-dependent Mg2+ and polyamine blockade and strong rectification. Two constrictions, at the inner helix bundle and at the apex of the cytoplasmic pore, may function as gates: in one structure the apex is open and in the other, it is closed. Gating of the apex is mediated by rigid-body movements of the cytoplasmic pore subunits. Phosphatidylinositol 4,5-biphosphate-interacting residues suggest a possible mechanism by which the signaling lipid regulates the cytoplasmic pore.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7601828
Ending Page	4015
Page Count	11
Starting Page	4005
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	17
Volume Number	26
Language	English
Publisher	Nature Publishing Group
Publisher Date	2007-09-05
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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