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- EMDB-44520: Cryo-EM structure of Trypanosoma cruzi MscS -

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Basic information

Entry
Database: EMDB / ID: EMD-44520
TitleCryo-EM structure of Trypanosoma cruzi MscS
Map datasharp
Sample
  • Complex: TcMscS
    • Protein or peptide: Mechanosensitive ion channel MscS domain-containing protein
Keywordsion channels / mechanosensitive channels / membrane protein / heptameric / TRANSPORT PROTEIN
Function / homologyMechanosensitive 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 speciesTrypanosoma cruzi (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.21 Å
AuthorsZhang J / Yuan P
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM143440 United States
CitationJournal: Nat Commun / Year: 2025
Title: 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.
History
DepositionApr 19, 2024-
Header (metadata) releaseMay 7, 2025-
Map releaseMay 7, 2025-
UpdateAug 20, 2025-
Current statusAug 20, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_44520.png

Downloads & links

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Map

FileDownload / File: emd_44520.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharp
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.2 Å/pix.
x 192 pix.
= 230.4 Å		1.2 Å/pix.
x 192 pix.
= 230.4 Å		1.2 Å/pix.
x 192 pix.
= 230.4 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.2 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 1.0
Minimum - Maximum-5.5852075 - 11.173448
Average (Standard dev.)0.00793564 (±0.25296447)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 230.40001 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: deepEMhancer

Fileemd_44520_additional_1.map
AnnotationdeepEMhancer
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Additional map: map

Fileemd_44520_additional_2.map
Annotationmap
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Half map: half A

Fileemd_44520_half_map_1.map
Annotationhalf_A
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Half map: half B

Fileemd_44520_half_map_2.map
Annotationhalf_B
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Sample components

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Entire : TcMscS

EntireName: TcMscS
Components
  • Complex: TcMscS
    • Protein or peptide: Mechanosensitive ion channel MscS domain-containing protein

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Supramolecule #1: TcMscS

SupramoleculeName: TcMscS / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: TcMscS in GDN
Source (natural)Organism: Trypanosoma cruzi (eukaryote)

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Macromolecule #1: Mechanosensitive ion channel MscS domain-containing protein

MacromoleculeName: Mechanosensitive ion channel MscS domain-containing protein
type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Trypanosoma cruzi (eukaryote)
Molecular weightTheoretical: 18.803393 KDa
Recombinant expressionOrganism: Komagataella pastoris (fungus)
SequenceString:
MKRFFNRFYL DTGIIADPSQ RSLASRVSAF LVQGAVAFSL LGTIGVDTSP LIAAAGVTGA TIGFACKDFG TNFVASIVLS GQQSIRTGN LVCIGTGLNV VKGKVVDWDT RYLYLRSSEG HLLHVPNNMV LNSVVTWEQE KKQNPHETDL PKQDVVKAPG D NAAKQSNS LEVLFQ

UniProtKB: Mechanosensitive ion channel MscS domain-containing protein

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
Component:
ConcentrationFormulaName
150.0 mMNaClsodium chloride
20.0 mMTrisTris
0.04 mMGDNglyco-diosgenin

Details: 20 mM Tris-HCl PH 8.0, 150 mM NaCl and 0.04 mM GDN
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number real images: 3269 / Average electron dose: 43.11 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm

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Image processing

Particle selectionNumber selected: 2193852
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL / In silico model: Alphafold
Final reconstructionApplied symmetry - Point group: C7 (7 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 229377
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
Output model

PDB-9bgq:
Cryo-EM structure of Trypanosoma cruzi MscS

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