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TitleCryo-electron microscopy structure of CLHM1 ion channel from Caenorhabditis elegans.
Journal, issue, pagesProtein Sci, Vol. 29, Issue 8, Page 1803-1815, Year 2020
Publish dateJun 30, 2020
AuthorsWeixin Yang / Youwang Wang / Jianli Guo / Lingli He / Ye Zhou / Hui Zheng / Zhenfeng Liu / Ping Zhu / Xuejun C Zhang /
PubMed AbstractCalcium 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.
External linksProtein Sci / PubMed:32557855 / PubMed Central
MethodsEM (single particle)
Resolution3.73 Å
Structure data

0938

6lom

EMDB-0938, PDB-6lom:
Structure of CLHM1 from Caenorhabditis Elegans
Method: EM (single particle) / Resolution: 3.73 Å

Source
  • caenorhabditis elegans (invertebrata)
KeywordsMEMBRANE PROTEIN / complex

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