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- EMDB-76005: EcMscM in NaCl in a closed conformation -

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Basic information

Entry
Database: EMDB / ID: EMD-76005
TitleEcMscM in NaCl in a closed conformation
Map data
Sample
  • Complex: MscM
    • Protein or peptide: Mechanosensitive channel of mini conductance MscM
KeywordsMechanosensitive / Ion channel / MscS / MEMBRANE PROTEIN
Function / homology
Function and homology information


mechanosensitive monoatomic ion channel activity / cellular response to osmotic stress / plasma membrane
Similarity search - Function
Mechanosensitive ion channel MscS, porin domain / Mechanosensitive ion channel inner membrane domain 1 / : / Mechanosensitive ion channel inner membrane domain 1 / Mechanosensitive ion channel porin domain / : / : / Mechanosensitive ion channel MscS, C-terminal / Mechanosensitive ion channel, transmembrane helices 2/3 / Mechanosensitive ion channel MscS, conserved site ...Mechanosensitive ion channel MscS, porin domain / Mechanosensitive ion channel inner membrane domain 1 / : / Mechanosensitive ion channel inner membrane domain 1 / Mechanosensitive ion channel porin domain / : / : / Mechanosensitive ion channel MscS, C-terminal / Mechanosensitive ion channel, transmembrane helices 2/3 / Mechanosensitive ion channel MscS, conserved site / Uncharacterized protein family UPF0003 signature. / Mechanosensitive ion channel MscS, C-terminal / 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
Miniconductance mechanosensitive channel MscM
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.7 Å
AuthorsHiotis G / Walz T
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)R01 GM144581 United States
CitationJournal: Nat Commun / Year: 2026
Title: 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.
History
DepositionMar 11, 2026-
Header (metadata) releaseAug 5, 2026-
Map releaseAug 5, 2026-
UpdateAug 5, 2026-
Current statusAug 5, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_76005.png

Downloads & links

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Map

FileDownload / File: emd_76005.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 450 pix.
= 381.15 Å		0.85 Å/pix.
x 450 pix.
= 381.15 Å		0.85 Å/pix.
x 450 pix.
= 381.15 Å

Surface

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.847 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.091
Minimum - Maximum-0.22098146 - 0.49775243
Average (Standard dev.)0.0037659444 (±0.018704562)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 381.15 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_76005_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_76005_half_map_2.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : MscM

EntireName: MscM
Components
  • Complex: MscM
    • Protein or peptide: Mechanosensitive channel of mini conductance MscM

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Supramolecule #1: MscM

SupramoleculeName: MscM / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli K-12 (bacteria)

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Macromolecule #1: Mechanosensitive channel of mini conductance MscM

MacromoleculeName: Mechanosensitive channel of mini conductance MscM / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
SequenceString: MRLIITFLMA WCLSWGAYAA TAPDSKQITQ ELEQAKAAKP AQPEVVEALQ SALNALEERK GSLERIKQYQ QVIDNYPKLS ATLRAQLNNM RDEPRSVSPG MSTDALNQEI LQVSSQLLDK SRQAQQEQER AREIADSLNQ LPQQQTDARR QLNEIERRLG TLTGNTPLNQ ...String:
MRLIITFLMA WCLSWGAYAA TAPDSKQITQ ELEQAKAAKP AQPEVVEALQ SALNALEERK GSLERIKQYQ QVIDNYPKLS ATLRAQLNNM RDEPRSVSPG MSTDALNQEI LQVSSQLLDK SRQAQQEQER AREIADSLNQ LPQQQTDARR QLNEIERRLG TLTGNTPLNQ AQNFALQSDS ARLKALVDEL ELAQLSANNR QELARLRSEL AEKESQQLDA YLQALRNQLN SQRQLEAERA LESTELLAEN SADLPKDIVA QFKINRELSA ALNQQAQRMD LVASQQRQAA SQTLQVRQAL NTLREQSQWL GSSNLLGEAL RAQVARLPEM PKPQQLDTEM AQLRVQRLRY EDLLNKQPLL RQIHQADGQP LTAEQNRILE AQLRTQRELL NSLLQGGDTL LLELTKLKVS NGQLEDALKE VNEATHRYLF WTSDVRPMTI AWPLEIAQDL RRLISLDTFS QLGKASVMML TSKETILPLF GALILVGCSI YSRRYFTRFL ERSAAKVGKV TQDHFWLTLR TLFWSILVAS PLPVLWMTLG YGLREAWPYP LAVAIGDGVT ATVPLLWVVM ICATFARPNG LFIAHFGWPR ERVSRGMRYY LMSIGLIVPL IMALMMFDNL DDREFSGSLG RLCFILICGA LAVVTLSLKK AGIPLYLNKE GSGDNITNHM LWNMMIGAPL VAILASAVGY LATAQALLAR LETSVAIWFL LLVVYHVIRR WMLIQRRRLA FDRAKHRRAE MLAQRARGEE EAHHHSSPEG AIEVDESEVD LDAISAQSLR LVRSILMLIA LLSVIVLWSE IHSAFGFLEN ISLWDVTSTV QGVESLEPIT LGAVLIAILV FIITTQLVRN LPALLELAIL QHLDLTPGTG YAITTITKYL LMLIGGLVGF SMIGIEWSKL QWLVAALGVG LGFGLQEIFA NFISGLIILF EKPIRIGDTV TIRDLTGSVT KINTRATTIS DWDRKEIIVP NKAFITEQFI NWSLSDSVTR VVLTIPAPAD ANSEEVTEIL LTAARRCSLV IDNPAPEVFL VDLQQGIQIF ELRIYAAEMG HRMPLRHEIH QLILAGFHAH GIDMPFPPFQ MRLESLNGKQ TGRTLTSAGK GRQAGSLLEV LFQGPGGSGG SMVSKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGDAT YGKLTLKFIC TTGKLPVPWP TLVTTLTYGV QCFSRYPDHM KQHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI DFKEDGNILG HKLEYNYNSH NVYIMADKQK NGIKVNFKIR HNIEDGSVQL ADHYQQNTPI GDGPVLLPDN HYLSTQSALS KDPNEKRDHM VLLEFVTAAG ITLGMDELYK HHHHHHHHHH

UniProtKB: Miniconductance mechanosensitive channel MscM

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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

Concentration7 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
150.0 mMNaClSodium Chloride
30.0 mMTris-HClTris(hydroxymethyl)aminomethane hydrochloride
0.02 mg/mlGDNGlyco-diosgenin
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
SoftwareName: SerialEM
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.2 sec. / Average electron dose: 46.21 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C7 (7 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 6.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 10378
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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