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Open data
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Basic information
| Entry | Database: PDB / ID: 11sm | ||||||||||||||||||||||||
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| Title | Core of EcMscM in NaCl in a closed conformation | ||||||||||||||||||||||||
Components | Miniconductance mechanosensitive channel MscM | ||||||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / Mechanosensitive / Ion channel / MscS | ||||||||||||||||||||||||
| Function / homology | Function and homology informationmechanosensitive monoatomic ion channel activity / cellular response to osmotic stress / plasma membrane Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||||||||||||||||||||
Authors | Hiotis, G. / Walz, T. | ||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: The bacterial mechanosensitive channel MscM gates through concerted changes in its transmembrane and cytoplasmic domains. Authors: Giorgos Hiotis / Thomas Walz / ![]() Abstract: The mechanosensitive channel of small conductance (MscS) is the founding member of the family of MscS-like channels, which share a structurally conserved core but feature additional structural ...The mechanosensitive channel of small conductance (MscS) is the founding member of the family of MscS-like channels, which share a structurally conserved core but feature additional structural elements that define their specific channel characteristics. Here, we characterize the structure and function of the Escherichia coli mechanosensitive channel of mini conductance (MscM), which features eight additional transmembrane (TM) helices and a large periplasmic domain. Our cryo-EM structures reveal that channel gating involves conformational changes in all domains of MscM. In particular, a cytoplasmic extension of TM7 couples the conformation of the TM domain to that of the cytoplasmic domain, resulting in gating of its lateral fenestrations, where ions enter the channel. Thus, different from all other MscS-like channels studied to date, channel gating in MscM is mediated by its cytoplasmic domain and not the TM domain, which senses changes in membrane tension and operates the cytoplasmic gates. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 11sm.cif.gz | 338 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb11sm.ent.gz | 212.1 KB | Display | PDB format |
| PDBx/mmJSON format | 11sm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1s/11sm ftp://data.pdbj.org/pub/pdb/validation_reports/1s/11sm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 76007MC ![]() 11soC ![]() 11sqC ![]() 11srC C: citing same article ( M: map data used to model this data |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 124824.023 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Komagataella pastoris (fungus) / Strain (production host): SMD1163H / References: UniProt: P39285Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: MscM / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: ![]() | ||||||||||||||||||||
| Source (recombinant) | Organism: Komagataella pastoris (fungus) / Strain: SMD1163H | ||||||||||||||||||||
| Buffer solution | pH: 7.4 | ||||||||||||||||||||
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| Specimen | Conc.: 7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Average exposure time: 1.2 sec. / Electron dose: 46.21 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C7 (7 fold cyclic) | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50627 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building | Source name: AlphaFold / Type: in silico model |
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About Yorodumi






United States, 1items
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PDBj


Komagataella pastoris (fungus)
FIELD EMISSION GUN