6LOM

Structure of CLHM1 from Caenorhabditis Elegans

Summary for 6LOM

• Entry DOI: 10.2210/pdb6lom/pdb
• EMDB information: 0938
• Descriptor: Calcium homeostasis modulator protein (1 entity in total)
• Functional Keywords: complex, membrane protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 20
• Total formula weight: 746172.66

Authors

Yang, W.X.,Wang, Y.W.,Zhang, X.C. (deposition date: 2020-01-06, release date: 2020-07-29, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.73 Å)