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TitleStructural insights into the activation mechanism of the human zinc-activated channel.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 442, Year 2025
Publish dateJan 7, 2025
AuthorsXuhang Lu / Dongmei Li / Yaojie Wang / Gaohua Zhang / Tianlei Wen / Yue Lu / Nan Jia / Xuedi Wang / Shenghai Chang / Xing Zhang / Jianping Lin / Yu-Hang Chen / Xue Yang / Yuequan Shen /
PubMed AbstractThe zinc-activated channel (ZAC) is an atypical mammalian cys-loop receptor (CLR) that is activated by zinc ions and protons, allowing cations to pass through. The molecular mechanism that ligands ...The zinc-activated channel (ZAC) is an atypical mammalian cys-loop receptor (CLR) that is activated by zinc ions and protons, allowing cations to pass through. The molecular mechanism that ligands use to activate ZAC remains elusive. Here, we present three cryo-electron microscopy reconstructions of human ZAC (hZAC) under different conditions. These three hZAC structures display highly similar conformations to one another, forming symmetrical homo-pentamers with a central ion-conduction pore. The hZAC protomer comprises an extracellular domain (ECD) and a transmembrane domain (TMD), sharing more structural similarity with anion-permeable CLRs, such as glycine receptors and type A γ-aminobutyric acid receptors. Notably, hZAC possesses a distinctive C-tail that establishes a disulfide bond with the loop M2-M3 in the TMD and occupies what is typically the canonical neurotransmitter orthosteric site in other mammalian CLRs. Moreover, the tip of the cys-loop creates an unprecedented orthosteric site in hZAC. The binding of Zn triggers a conformational shift in the cys-loop, which presumably prompts the loop M2-M3 to move and open the channel gate. This study sheds light on the assembly of the channel, its structural features, and the process of signal transduction in hZAC.
External linksNat Commun / PubMed:39774710 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 2.9 Å
Structure data

39648

8yx6

EMDB-39648, PDB-8yx6:
Structure of a Cys-loop Receptor in Zinc Binding State
Method: EM (single particle) / Resolution: 2.9 Å

39649

8yx7

EMDB-39649, PDB-8yx7:
Structure of a Cys-loop Receptor under Acidic Condition
Method: EM (single particle) / Resolution: 2.8 Å

39650

8yx8

EMDB-39650, PDB-8yx8:
Structure of a Cys-loop Receptor in Apo State
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

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

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Cys-loop Receptor

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