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- EMDB-55971: cryo-EM structure of MscL G22S mutant from Escherichia coli in MS... -

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Basic information

Entry
Database: EMDB / ID: EMD-55971
Titlecryo-EM structure of MscL G22S mutant from Escherichia coli in MSP nanodisc
Map data
Sample
  • Organelle or cellular component: MscL
    • Protein or peptide: Large-conductance mechanosensitive channel
KeywordsMechanosensitive channel / MEMBRANE PROTEIN
Function / homology
Function and homology information


intracellular water homeostasis / mechanosensitive monoatomic ion channel activity / monoatomic ion transport / monoatomic ion transmembrane transport / membrane / identical protein binding / plasma membrane
Similarity search - Function
Large-conductance mechanosensitive channel / Large-conductance mechanosensitive channel, conserved site / Large-conductance mechanosensitive channels mscL family signature. / Large-conductance mechanosensitive channel MscL / Large-conductance mechanosensitive channel/anditomin synthesis protein L / Large-conductance mechanosensitive channel, MscL
Similarity search - Domain/homology
Large-conductance mechanosensitive channel
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.46 Å
AuthorsXiao T / Sprink T / Lange A
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG)EXC 2008 1 UniSysCat 390540038 Germany
CitationJournal: Sci Adv / Year: 2026
Title: Atomic structure and dynamics of the mechanosensitive channel MscL from by cryo-EM and solid-state NMR.
Authors: Taoran Xiao / Alexandra Kovinko / Chaowei Shi / Henry Sawczyc / Denis Qoraj / Carl Öster / Thiemo Sprink / Anton F Ketzel / Sascha Lange / Spyridon Kosteletos / Han Sun / Daniel Roderer / ...Authors: Taoran Xiao / Alexandra Kovinko / Chaowei Shi / Henry Sawczyc / Denis Qoraj / Carl Öster / Thiemo Sprink / Anton F Ketzel / Sascha Lange / Spyridon Kosteletos / Han Sun / Daniel Roderer / Shanshuang Chen / Adam Lange /
Abstract: Mechanosensitive channels are central to cellular responses to membrane tension, yet the structural basis of their gating remains incompletely understood. Here, we determine the structures of wild- ...Mechanosensitive channels are central to cellular responses to membrane tension, yet the structural basis of their gating remains incompletely understood. Here, we determine the structures of wild-type and Gly22→Ser (G22S) mutants of MscL from (MscL) by cryogenic electron microscopy (cryo-EM) in peptide-based lipid nanodiscs and complement them with solid-state nuclear magnetic resonance (NMR) measurements in liposomes to capture their dynamics in a native-like membrane environment. The cryo-EM structures reveal a closed conformation, whereas analysis of the low-threshold G22S mutant by NMR uncovers widespread conformational changes in both cytoplasmic and periplasmic regions. These data indicate enhanced dynamics and conformational heterogeneity in the mutant, revealing the early transitions from the closed toward the open state. Together, our results establish a synergistic framework integrating cryo-EM and NMR to resolve both structure and dynamics of mechanosensitive channels, and identify lipid-protein interactions as key determinants of MscL gating and mechanosensitivity. Our study further provides a quantitative benchmark for computational investigations of mechanogating and lays the foundation for the rational design of channels with tunable gating kinetics.
History
DepositionDec 5, 2025-
Header (metadata) releaseSep 9, 2026-
Map releaseSep 9, 2026-
UpdateOct 21, 2026-
Current statusOct 21, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55971.png

Downloads & links

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Map

FileDownload / File: emd_55971.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
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AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 360 pix.
= 298.8 Å		0.83 Å/pix.
x 360 pix.
= 298.8 Å		0.83 Å/pix.
x 360 pix.
= 298.8 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
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Contour LevelBy AUTHOR: 0.08
Minimum - Maximum-0.040522654 - 0.22049822
Average (Standard dev.)0.0001484218 (±0.0065598693)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 298.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_55971_msk_1.map
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Additional map: deepEMhancer tightTarget

Fileemd_55971_additional_1.map
AnnotationdeepEMhancer_tightTarget
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Half map: #2

Fileemd_55971_half_map_1.map
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Half map: #1

Fileemd_55971_half_map_2.map
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Sample components

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Entire : MscL

EntireName: MscL
Components
  • Organelle or cellular component: MscL
    • Protein or peptide: Large-conductance mechanosensitive channel

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Supramolecule #1: MscL

SupramoleculeName: MscL / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli)

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Macromolecule #1: Large-conductance mechanosensitive channel

MacromoleculeName: Large-conductance mechanosensitive channel / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 15.002737 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSIIKEFREF AMRGNVVDLA VSVIIGAAFG KIVSSLVADI IMPPLGLLIG GIDFKQFAVT LRDAQGDIPA VVMHYGVFIQ NVFDFLIVA FAIFMAIKLI NKLNRKKEEP AAAPAPTKEE VLLTEIRDLL KEQNNRS

UniProtKB: Large-conductance mechanosensitive channel

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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

Concentration0.4 mg/mL
BufferpH: 7.4 / Details: 20 mM HEPES, pH 7.4,100 mM KCl
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average exposure time: 0.9 sec. / Average electron dose: 60.1 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.46 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 1049338
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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