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TitleCryo-EM structure of the calcium homeostasis modulator 1 channel.
Journal, issue, pagesSci Adv, Vol. 6, Issue 29, Page eaba8161, Year 2020
Publish dateJul 17, 2020
AuthorsYue Ren / Tianlei Wen / Zhiqin Xi / Shunjin Li / Jing Lu / Xing Zhang / Xue Yang / Yuequan Shen /
PubMed AbstractCalcium homeostasis modulator 1 (CALHM1) is a voltage-gated ATP release channel that plays an important role in neural gustatory signaling and the pathogenesis of Alzheimer's disease. Here, we ...Calcium homeostasis modulator 1 (CALHM1) is a voltage-gated ATP release channel that plays an important role in neural gustatory signaling and the pathogenesis of Alzheimer's disease. Here, we present a cryo-electron microscopy structure of full-length Ca-free CALHM1 from Danio rerio at an overall resolution of 3.1 Å. Our structure reveals an octameric architecture with a wide pore diameter of ~20 Å, presumably representing the active conformation. The overall structure is substantially different from that of the isoform CALHM2, which forms both undecameric hemichannels and gap junctions. The N-terminal small helix folds back to the pore and forms an antiparallel interaction with transmembrane helix 1. Structural analysis revealed that the extracellular loop 1 region within the dimer interface may contribute to oligomeric assembly. A positive potential belt inside the pore was identified that may modulate ion permeation. Our structure offers insights into the assembly and gating mechanism of the CALHM1 channel.
External linksSci Adv / PubMed:32832630 / PubMed Central
MethodsEM (single particle)
Resolution3.1 Å
Structure data

30016

6lyg

EMDB-30016, PDB-6lyg:
Cryo-EM structure of the calcium homeostasis modulator 1 channel
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • danio rerio (zebrafish)
KeywordsMEMBRANE PROTEIN / Octamer

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