Database: EMDB / ID: EMD-26823
|Title||EcMscK G924S mutant in a closed conformation|
|Map data||EcMscK G924S mutant in a closed conformation|
|Function / homology|
Function and homology information
intracellular water homeostasis / mechanosensitive monoatomic ion channel activity / response to potassium ion / potassium ion transport / 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, conserved site / Uncharacterized protein family UPF0003 signature. / Mechanosensitive ion channel MscS, C-terminal / Mechanosensitive ion channel MscS / Mechanosensitive ion channel MscS, transmembrane-2 / Mechanosensitive ion channel ...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, conserved site / Uncharacterized protein family UPF0003 signature. / Mechanosensitive ion channel MscS, C-terminal / Mechanosensitive ion channel MscS / Mechanosensitive ion channel MscS, transmembrane-2 / Mechanosensitive ion channel / Mechanosensitive ion channel MscS, beta-domain superfamily / LSM domain superfamily / P-type ATPase, transmembrane domain superfamily
Similarity search - Domain/homology
Mechanosensitive channel MscK
Similarity search - Component
|Biological species||Escherichia coli K-12 (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.84 Å|
|Authors||Mount JW / Yuan P|
|Funding support|| United States, 1 items |
|Citation||Journal: Nat Commun / Year: 2022|
Title: Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel.
Authors: Jonathan Mount / Grigory Maksaev / Brock T Summers / James A J Fitzpatrick / Peng Yuan /
Abstract: Mechanosensitive channels of small conductance, found in many living organisms, open under elevated membrane tension and thus play crucial roles in biological response to mechanical stress. Amongst ...Mechanosensitive channels of small conductance, found in many living organisms, open under elevated membrane tension and thus play crucial roles in biological response to mechanical stress. Amongst these channels, MscK is unique in that its activation also requires external potassium ions. To better understand this dual gating mechanism by force and ligand, we elucidate distinct structures of MscK along the gating cycle using cryo-electron microscopy. The heptameric channel comprises three layers: a cytoplasmic domain, a periplasmic gating ring, and a markedly curved transmembrane domain that flattens and expands upon channel opening, which is accompanied by dilation of the periplasmic ring. Furthermore, our results support a potentially unifying mechanotransduction mechanism in ion channels depicted as flattening and expansion of the transmembrane domain.
Downloads & links
|File||Download / File: emd_26823.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Annotation||EcMscK G924S mutant in a closed conformation|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.94 Å|
|Symmetry||Space group: 1|
-Half map: EcMscK G924S mutant in a closed conformation, half map A
|Annotation||EcMscK G924S mutant in a closed conformation, half map A|
|Projections & Slices|
-Half map: EcMscK G924S mutant in a closed conformation, half map B
-Entire : E.coli MscK
|Entire||Name: E.coli MscK|
-Supramolecule #1: E.coli MscK
|Supramolecule||Name: E.coli MscK / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Homomeric Heptamer|
|Source (natural)||Organism: Escherichia coli K-12 (bacteria) / Location in cell: Inner Membrane|
|Recombinant expression||Organism: Komagataella pastoris (fungus) / Recombinant plasmid: PV-1|
-Macromolecule #1: Mechanosensitive channel MscK
|Macromolecule||Name: Mechanosensitive channel MscK / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO|
|Source (natural)||Organism: Escherichia coli K-12 (bacteria) / Strain: K12|
|Molecular weight||Theoretical: 127.378789 KDa|
|Recombinant expression||Organism: Komagataella pastoris (fungus)|
|Sequence||String: MTMFQYYKRS RHFVFSAFIA FVFVLLCQNT AFARASSNGD LPTKADLQAQ LDSLNKQKDL SAQDKLVQQD LTDTLATLDK IDRIKEETV QLRQKVAEAP EKMRQATAAL TALSDVDNDE ETRKILSTLS LRQLETRVAQ ALDDLQNAQN DLASYNSQLV S LQTQPERV ...String: |
MTMFQYYKRS RHFVFSAFIA FVFVLLCQNT AFARASSNGD LPTKADLQAQ LDSLNKQKDL SAQDKLVQQD LTDTLATLDK IDRIKEETV QLRQKVAEAP EKMRQATAAL TALSDVDNDE ETRKILSTLS LRQLETRVAQ ALDDLQNAQN DLASYNSQLV S LQTQPERV QNAMYNASQQ LQQIRSRLDG TDVGETALRP SQKVLMQAQQ ALLNAEIDQQ RKSLEGNTVL QDTLQKQRDY VT ANSARLE HQLQLLQEAV NSKRLTLTEK TAQEAVSPDE AARIQANPLV KQELEINQQL SQRLITATEN GNQLMQQNIK VKN WLERAL QSERNIKEQI AVLKGSLLLS RILYQQQQTL PSADELENMT NRIADLRLEQ FEVNQQRDAL FQSDAFVNKL EEGH TNEVN SEVHDALLQV VDMRRELLDQ LNKQLGNQLM MAINLQINQQ QLMSVSKNLK SILTQQIFWV NSNRPMDWDW IKAFP QSLK DEFKSMKITV NWQKAWPAVF IAFLAGLPLL LIAGLIHWRL GWLKAYQQKL ASAVGSLRND SQLNTPKAIL IDLIRA LPV CLIILAVGLI LLTMQLNISE LLWSFSKKLA IFWLVFGLCW KVLEKNGVAV RHFGMPEQQT SHWRRQIVRI SLALLPI HF WSVVAELSPL HLMDDVLGQA MIFFNLLLIA FLVWPMCRES WRDKESHTMR LVTITVLSII PIALMVLTAT GYFYTTLR L AGRWIETVYL VIIWNLLYQT VLRGLSVAAR RIAWRRALAR RQNLVKEGAE GAEPPEEPTI ALEQVNQQTL RITMLLMFA LFGVMFWAIW SDLITVFSYL DSITLWHYNG TEAGAAVVKN VTMGSLLFAI IASMVAWALI RNLPGLLEVL VLSRLNMRQG ASYAITTIL NYIIIAVGAM TVFGSLGVSW DKLQWLAAAL SVGLSFGLQE IFGNFVSGLI ILFERPVRIG DTVTIGSFSG T VSKIRIRA TTITDFDRKE VIIPNKAFVT ERLINWSLTD TTTRLVIRLG VAYGSDLEKV RKVLLKAATE HPRVMHEPMP EV FFTAFGA STLDHELRLY VRELRDRSRT VDELNRTIDQ LCRENDINIA FNQLEVHLHN EKGDEVTEVK RDYKGDDPTP AVG
|Processing||single particle reconstruction|
|Buffer||pH: 8 |
Details: Micrographs were pooled from protein purified in the presence of either 150mM NaCl or 150mM KCl, respectively. Buffers were prepared fresh, degassed, and filtered through a 0.45 um Durapore PVDF membrane
|Grid||Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE|
|Vitrification||Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV|
|Details||The specimen was homogeneous and monodisperse.|
|Electron beam||Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 150000|
|Sample stage||Cooling holder cryogen: NITROGEN|
|Image recording||Film or detector model: FEI FALCON IV (4k x 4k) / Detector mode: COUNTING / Average electron dose: 46.16 e/Å2|
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