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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of Trypanosoma cruzi MscS C66L in nanodiscs | |||||||||
Map data | sharp | |||||||||
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Keywords | ion channels / mechanosensitive channels / membrane protein / heptameric / TRANSPORT PROTEIN | |||||||||
| Function / homology | Mechanosensitive ion channel MscS, archaea/bacteria type / Mechanosensitive ion channel MscS, transmembrane-2 / Mechanosensitive ion channel MscS / Mechanosensitive ion channel, beta-domain / Mechanosensitive ion channel MscS, beta-domain superfamily / mechanosensitive monoatomic ion channel activity / LSM domain superfamily / membrane / Mechanosensitive ion channel MscS domain-containing protein Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.39 Å | |||||||||
Authors | Zhang J / Yuan P | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2025Title: Lipid-mediated gating of a miniature mechanosensitive MscS channel from Trypanosoma cruzi. Authors: Jingying Zhang / Aashish Bhatt / Grigory Maksaev / Yun Lyna Luo / Peng Yuan / ![]() Abstract: The mechanosensitive channel of small conductance (MscS) from E. coli (EcMscS) has served as the prevailing model system for understanding mechanotransduction in ion channels. Trypanosoma cruzi, the ...The mechanosensitive channel of small conductance (MscS) from E. coli (EcMscS) has served as the prevailing model system for understanding mechanotransduction in ion channels. Trypanosoma cruzi, the protozoan parasite causing Chagas disease, encodes a miniature MscS ortholog (TcMscS) critical for parasite development and infectivity. TcMscS contains a minimal portion of the canonical EcMscS fold yet maintains mechanosensitive channel activity, thus presenting a unique model system to assess the essential molecular determinants underlying mechanotransduction. Using cryo-electron microscopy and molecular dynamics simulations, we show that TcMscS contains two short membrane-embedded helices that would not fully cross an intact lipid bilayer. Consequently, drastic membrane deformation is induced at the protein-lipid interface, resulting in a funnel-shaped bilayer surrounding the channel. Resident lipids within the central pore lumen block ion permeation pathway, and their departure driven by lateral membrane tension is required for ion conduction. Together with electrophysiology and mutagenesis studies, our results support a direct lipid-mediated mechanical gating transition. Moreover, these findings provide a foundation for the development of alternative treatment of Chagas disease by inhibition of the TcMscS channel. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_44522.map.gz | 32.3 MB | EMDB map data format | |
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| Header (meta data) | emd-44522-v30.xml emd-44522.xml | 20.8 KB 20.8 KB | Display Display | EMDB header |
| Images | emd_44522.png | 119.5 KB | ||
| Filedesc metadata | emd-44522.cif.gz | 6.1 KB | ||
| Others | emd_44522_additional_1.map.gz emd_44522_half_map_1.map.gz emd_44522_half_map_2.map.gz | 17.1 MB 31.9 MB 31.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-44522 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-44522 | HTTPS FTP |
-Validation report
| Summary document | emd_44522_validation.pdf.gz | 875.4 KB | Display | EMDB validaton report |
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| Full document | emd_44522_full_validation.pdf.gz | 875 KB | Display | |
| Data in XML | emd_44522_validation.xml.gz | 11 KB | Display | |
| Data in CIF | emd_44522_validation.cif.gz | 12.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44522 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44522 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9bgtMC ![]() 9bgqC ![]() 9bgsC ![]() 9bguC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_44522.map.gz / Format: CCP4 / Size: 34.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | sharp | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.083 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: map
| File | emd_44522_additional_1.map | ||||||||||||
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| Annotation | map | ||||||||||||
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| Density Histograms |
-Half map: half A
| File | emd_44522_half_map_1.map | ||||||||||||
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| Annotation | half_A | ||||||||||||
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| Density Histograms |
-Half map: half B
| File | emd_44522_half_map_2.map | ||||||||||||
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| Annotation | half_B | ||||||||||||
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Sample components
-Entire : TcMscS C66L in nanodiscs
| Entire | Name: TcMscS C66L in nanodiscs |
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| Components |
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-Supramolecule #1: TcMscS C66L in nanodiscs
| Supramolecule | Name: TcMscS C66L in nanodiscs / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Mechanosensitive ion channel MscS domain-containing protein
| Macromolecule | Name: Mechanosensitive ion channel MscS domain-containing protein type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 18.813408 KDa |
| Recombinant expression | Organism: Komagataella pastoris (fungus) |
| Sequence | String: MKRFFNRFYL DTGIIADPSQ RSLASRVSAF LVQGAVAFSL LGTIGVDTSP LIAAAGVTGA TIGFALKDFG TNFVASIVLS GQQSIRTGN LVCIGTGLNV VKGKVVDWDT RYLYLRSSEG HLLHVPNNMV LNSVVTWEQE KKQNPHETDL PKQDVVKAPG D NAAKQSNS LEVLFQ UniProtKB: Mechanosensitive ion channel MscS domain-containing protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 Component:
Details: 20 mM Tris-HCl PH 8.0, 150 mM NaCl | |||||||||
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE | |||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 5985 / Average electron dose: 54.33 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
United States, 1 items
Citation








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Komagataella pastoris (fungus)
Processing
FIELD EMISSION GUN
