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

Chiu, Po-Lin and Pagel, Matthew D. and Evans, James and Chou, Hui-Ting and Zeng, Xiangyan and Gipson, Bryant and Stahlberg, Henning and Nimigean, Crina M.. (2007) The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution. Structure: with folding and design, Vol. 15, H. 9. pp. 1053-1064.

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Official URL: http://edoc.unibas.ch/dok/A5842556

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Current Biology
ISSN:0969-2126
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:55
Deposited On:08 Jun 2012 06:46

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