- EMDB-0938: Structure of CLHM1 from Caenorhabditis Elegans -
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Basic information
Entry
Database: EMDB / ID: EMD-0938
Title
Structure of CLHM1 from Caenorhabditis Elegans
Map data
Sample
Complex: predicted: CALHM1-like protein
Protein or peptide: Calcium homeostasis modulator protein
Function / homology
Function and homology information
non-motile cilium / regulation of monoatomic ion transmembrane transport / regulation of locomotion / voltage-gated calcium channel activity / monoatomic cation channel activity / calcium ion transmembrane transport / plasma membrane Similarity search - Function
Journal: Protein Sci / Year: 2020 Title: Cryo-electron microscopy structure of CLHM1 ion channel from Caenorhabditis elegans. Authors: Weixin Yang / Youwang Wang / Jianli Guo / Lingli He / Ye Zhou / Hui Zheng / Zhenfeng Liu / Ping Zhu / Xuejun C Zhang / 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- ...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.
History
Deposition
Jan 6, 2020
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Header (metadata) release
Jul 29, 2020
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Map release
Jul 29, 2020
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Update
Aug 5, 2020
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Current status
Aug 5, 2020
Processing site: PDBj / Status: Released
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Structure visualization
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Surface view with section colored by density value
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