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Structure. 2007 Sep;15(9):1053-64.

The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution.

Author information

1
Molecular and Cellular Biology, College of Biological Sciences, University of California-Davis, 1 Shields Avenue, Davis, CA 95616, USA.

Abstract

The gating ring of cyclic nucleotide-modulated channels is proposed to be either a two-fold symmetric dimer of dimers or a four-fold symmetric tetramer based on high-resolution structure data of soluble cyclic nucleotide-binding domains and functional data on intact channels. We addressed this controversy by obtaining structural data on an intact, full-length, cyclic nucleotide-modulated potassium channel, MloK1, from Mesorhizobium loti, which also features a putative voltage-sensor. We present here the 3D single-particle structure by transmission electron microscopy and the projection map of membrane-reconstituted 2D crystals of MloK1 in the presence of cAMP. Our data show a four-fold symmetric arrangement of the CNBDs, separated by discrete gaps. A homology model for full-length MloK1 suggests a vertical orientation for the CNBDs. The 2D crystal packing in the membrane-embedded state is compatible with the S1-S4 domains in the vertical "up" state.

PMID:
17850745
PMCID:
PMC2000844
DOI:
10.1016/j.str.2007.06.020
[Indexed for MEDLINE]
Free PMC Article

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