6LOM

Structure of CLHM1 from Caenorhabditis Elegans

6LOM の概要

• エントリーDOI: 10.2210/pdb6lom/pdb
• EMDBエントリー: 0938
• 分子名称: Calcium homeostasis modulator protein (1 entity in total)
• 機能のキーワード: complex, membrane protein
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 746172.66

構造登録者

Yang, W.X.,Wang, Y.W.,Zhang, X.C. (登録日: 2020-01-06, 公開日: 2020-07-29, 最終更新日: 2024-11-20)

主引用文献

Yang, W.,Wang, Y.,Guo, J.,He, L.,Zhou, Y.,Zheng, H.,Liu, Z.,Zhu, P.,Zhang, X.C.
Cryo-electron microscopy structure of CLHM1 ion channel from Caenorhabditis elegans.
Protein Sci., 29:1803-1815, 2020

PubMed Abstract: Calcium homeostasis modulators (CALHMs/CLHMs) comprise a family of pore-forming protein complexes assembling into voltage-gated, Ca -sensitive, nonselective channels. These complexes contain an ion-conduction pore sufficiently wide to permit the passing of ATP molecules serving as neurotransmitters. While their function and structure information is accumulating, the precise mechanisms of these channel complexes remain to be full understood. Here, we present the structure of the Caenorhabditis elegans CLHM1 channel in its open state solved through single-particle cryo-electron microscopy at 3.7-Å resolution. The transmembrane region of the channel structure of the dominant class shows an assembly of 10-fold rotational symmetry in one layer, and its cytoplasmic region is involved in additional twofold symmetrical packing in a tail-to-tail manner. Furthermore, we identified a series of amino acid residues critical for the regulation of CeCLHM1 channel using functional assays, electrophysiological analyses as well as structural-based analysis. Our structure and function analyses provide new insights into the mechanisms of CALHM channels.

PubMed: 32557855
DOI: 10.1002/pro.3904

実験手法

ELECTRON MICROSCOPY (3.73 Å)