8WGE
Cryo-EM structure of the ZAC zinc-activated channel in the Cys-loop receptor superfamily
Summary for 8WGE
| Entry DOI | 10.2210/pdb8wge/pdb |
| EMDB information | 37511 |
| Descriptor | ZAC, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | channel, transport protein |
| Biological source | Oryzias latipes |
| Total number of polymer chains | 5 |
| Total formula weight | 237385.32 |
| Authors | Jin, F.,Hattori, M. (deposition date: 2023-09-21, release date: 2024-09-25, Last modification date: 2024-11-13) |
| Primary citation | Jin, F.,Lin, Y.Y.,Wang, R.C.,Xie, T.X.,Zhao, Y.,Shen, C.,Sheng, D.,Ichikawa, M.,Yu, Y.,Wang, J.,Hattori, M. Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily. Proc.Natl.Acad.Sci.USA, 121:e2405659121-e2405659121, 2024 Cited by PubMed Abstract: Cys-loop receptors are a large superfamily of pentameric ligand-gated ion channels with various physiological roles, especially in neurotransmission in the central nervous system. Among them, zinc-activated channel (ZAC) is a Zn-activated ion channel that is widely expressed in the human body and is conserved among eukaryotes. Due to its gating by extracellular Zn, ZAC has been considered a Zn sensor, but it has undergone minimal structural and functional characterization since its molecular cloning. Among the families in the Cys-loop receptor superfamily, only the structure of ZAC has yet to be determined. Here, we determined the cryo-EM structure of ZAC in the apo state and performed structure-based mutation analyses. We identified a few residues in the extracellular domain whose mutations had a mild impact on Zn sensitivity. The constriction site in the ion-conducting pore differs from the one in other Cys-loop receptor structures, and further mutational analysis identified a key residue that is important for ion selectivity. In summary, our work provides a structural framework for understanding the ion-conducting mechanism of ZAC. PubMed: 39441630DOI: 10.1073/pnas.2405659121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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