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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of a Cys-loop Receptor under Acidic Condition | |||||||||
![]() | EM_map | |||||||||
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![]() | Cys-loop Receptor / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() pH-gated monoatomic ion channel activity / transmembrane transporter complex / ligand-gated monoatomic ion channel activity / response to zinc ion / ligand-gated monoatomic cation channel activity / extracellular ligand-gated monoatomic ion channel activity / transmembrane signaling receptor activity / monoatomic ion transmembrane transport / zinc ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
![]() | Lu XH / Yang X / Shen YQ | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the activation mechanism of the human zinc-activated channel. Authors: Xuhang 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 / ![]() Abstract: 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 ...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. | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 42.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.7 KB 17.7 KB | Display Display | ![]() |
Images | ![]() | 134.7 KB | ||
Filedesc metadata | ![]() | 6.2 KB | ||
Others | ![]() ![]() | 77.6 MB 77.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 13 KB | Display | |
Data in CIF | ![]() | 15.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8yx7MC ![]() 8yx6C ![]() 8yx8C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | EM_map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.93 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Cys-loop Receptor under Acidic Condition
Entire | Name: Cys-loop Receptor under Acidic Condition |
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Components |
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-Supramolecule #1: Cys-loop Receptor under Acidic Condition
Supramolecule | Name: Cys-loop Receptor under Acidic Condition / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 230 KDa |
-Macromolecule #1: Ligand-gated cation channel ZACN
Macromolecule | Name: Ligand-gated cation channel ZACN / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 46.858117 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MMALWSLLHL TFLGFSITLL LVHGQGFQGT AAIWPSDYKD DDDKLFNVNL SKKVQESIQI PNNGSAPLLV DVRVFVSNVF NVDILRYTM SSMLLLRLSW LDTRLAWNTS AHPRHAITLP WESLWTPRLT ILEALWVDWR DQSPQARVDQ DGHVKLNLAL A TETNCNFE ...String: MMALWSLLHL TFLGFSITLL LVHGQGFQGT AAIWPSDYKD DDDKLFNVNL SKKVQESIQI PNNGSAPLLV DVRVFVSNVF NVDILRYTM SSMLLLRLSW LDTRLAWNTS AHPRHAITLP WESLWTPRLT ILEALWVDWR DQSPQARVDQ DGHVKLNLAL A TETNCNFE LLHFPRDHSN CSLSFYALSN TAMELEFQAH VVNEIVSVKR EYVVYDLKTQ VPPQQLVPCF QVTLRLKNTA LK SIIALLV PAEALLLADV CGGLLPLRAI ERIGYKVTLL LSYLVLHSSL VQALPSSSSC NPLLIYYFTI LLLLLFLSTI ETV LLAGLL ARGNLGAKSG PSPAPRGEQR EHGNPGPHPA EEPSRGVKGS QRSWPETADR IFFLVYVVGV LCTQFVFAGI WMWA ACKSD AAPGEAAPHG RRPRL UniProtKB: Ligand-gated cation channel ZACN |
-Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 5 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 10 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 288 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.3 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |