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- PDB-9sed: mechanosensitive channel MscS from Francisella tularensis, mutant K70A -

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Basic information

Entry
Database: PDB / ID: 9sed
Titlemechanosensitive channel MscS from Francisella tularensis, mutant K70A
ComponentsSmall-conductance mechanosensitive channel
KeywordsMEMBRANE PROTEIN / mechanosensitive channel / lipid interaction / bacteria
Function / homology
Function and homology information


mechanosensitive monoatomic ion channel activity / plasma membrane
Similarity search - Function
Conserved TM helix / Mechanosensitive ion channel, conserved TM helix / 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 / LSM domain superfamily
Similarity search - Domain/homology
TETRADECANE / DODECANE / N-OCTANE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / Small-conductance mechanosensitive channel
Similarity search - Component
Biological speciesFrancisella tularensis (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.77 Å
AuthorsRasmussen, A. / Hemmelmann, N. / Hove, T.T. / Flegler, V.J. / Rasmussen, T. / Bottcher, B.
Funding support Germany, 4items
OrganizationGrant numberCountry
German Research Foundation (DFG)538122946 Germany
German Research Foundation (DFG)359471283 Germany
German Research Foundation (DFG)525040890 Germany
German Research Foundation (DFG)456578072 Germany
CitationJournal: to be published
Title: An asymmetric gate in the homoheptameric mechanosensitive channel MscS from Francisella tularensis
Authors: Rasmussen, A. / Hemmelmann, N. / Bahner, J. / Hove, T.T. / Flegler, V.J. / Kraft, C. / Hedrich, R. / Rasmussen, T. / Bottcher, B.
History
DepositionAug 16, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 26, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 26, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Small-conductance mechanosensitive channel
B: Small-conductance mechanosensitive channel
C: Small-conductance mechanosensitive channel
D: Small-conductance mechanosensitive channel
E: Small-conductance mechanosensitive channel
F: Small-conductance mechanosensitive channel
G: Small-conductance mechanosensitive channel
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,57249
Polymers130,2057
Non-polymers11,36642
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Small-conductance mechanosensitive channel


Mass: 18600.771 Da / Num. of mol.: 7 / Mutation: K70A
Source method: isolated from a genetically manipulated source
Details: point mutation K70A, C-terminal His6-tag / Source: (gene. exp.) Francisella tularensis (bacteria) / Gene: FWI86_02060, FWJ04_01320 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0B3VCY4
#2: Chemical
ChemComp-PEE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE


Mass: 744.034 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C41H78NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: DOPE, phospholipid*YM
#3: Chemical
ChemComp-OCT / N-OCTANE


Mass: 114.229 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C8H18 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical...
ChemComp-C14 / TETRADECANE


Mass: 198.388 Da / Num. of mol.: 21 / Source method: obtained synthetically / Formula: C14H30 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-D12 / DODECANE


Mass: 170.335 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C12H26 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: homoheptameric complex of detergent solubilised MscS / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Molecular weightValue: 0.13 MDa / Experimental value: NO
Source (natural)Organism: Francisella tularensis (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
Buffer component
IDConc.NameFormulaBuffer-ID
150 mMHEPESC8H18N2O4S1
2150 mMsodium chlorideNaCl1
30.03 %DDMC24H46O111
45 mMEDTAC10H16N2O81
SpecimenConc.: 2.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 75000 X / Nominal defocus max: 1700 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 75 sec. / Electron dose: 80 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 1683

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.7particle selection
2EPU3.7.0image acquisition
4cryoSPARC4.7CTF correction
7Coot0.9.8.93model fitting
9cryoSPARC4.7initial Euler assignment
10cryoSPARC4.7final Euler assignment
12cryoSPARC4.73D reconstruction
13PHENIX1.20.1_4487model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 908293
SymmetryPoint symmetry: C7 (7 fold cyclic)
3D reconstructionResolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 137361 / Algorithm: FOURIER SPACE / Symmetry type: POINT
Atomic model buildingB value: 53 / Protocol: AB INITIO MODEL / Space: REAL
Atomic model buildingPDB-ID: 6RLD

6rld


Accession code: 6RLD / Source name: PDB / Type: experimental model
RefinementHighest resolution: 2.77 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039093
ELECTRON MICROSCOPYf_angle_d0.43312138
ELECTRON MICROSCOPYf_dihedral_angle_d5.9421687
ELECTRON MICROSCOPYf_chiral_restr0.041477
ELECTRON MICROSCOPYf_plane_restr0.0021386

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