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-Structure paper
タイトル | The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution. |
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ジャーナル・号・ページ | Structure, Vol. 15, Issue 9, Page 1053-1064, Year 2007 |
掲載日 | 2007年11月13日 |
著者 | Po-Lin Chiu / Matthew D Pagel / James Evans / Hui-Ting Chou / Xiangyan Zeng / Bryant Gipson / Henning Stahlberg / Crina M Nimigean / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:17850745 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 16.3 Å |
構造データ | EMDB-1424: |
由来 |
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