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Open data
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Basic information
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Title | Cryo-EM structure of MscS/YnaI chimera in DOPC nanodiscs | |||||||||
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![]() | Mechanosensitive / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() intracellular water homeostasis / mechanosensitive monoatomic ion channel activity / protein homooligomerization / monoatomic ion transmembrane transport / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.5 Å | |||||||||
![]() | Hiotis G / Will N / Walz T | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI. Authors: Nathan Will / Giorgos Hiotis / Yoshitaka Nakayama / Gabriella Angiulli / Zijing Zhou / Charles D Cox / Boris Martinac / Thomas Walz / ![]() ![]() Abstract: YnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been ...YnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been extensively studied for MscS, but are less well understood for YnaI, which features two additional transmembrane helices. Here, we combined cryogenic electron microscopy, molecular dynamics simulations and patch-clamp electrophysiology to advance our understanding of YnaI. The two additional helices move the lipid-filled hydrophobic pockets in YnaI further away from the lipid bilayer and change the function of the pocket lipids from being a critical gating element in MscS to being more of a structural element in YnaI. Unlike MscS, YnaI shows pronounced gating hysteresis and remains open to a substantially lower membrane tension than is needed to initially open the channel. Thus, at near-lytic membrane tension, both MscL and YnaI will open, but while MscL has a large pore and must close quickly to minimize loss of essential metabolites, YnaI only conducts ions and can thus remain open for longer to continue to facilitate pressure equilibration across the membrane. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 89 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.3 KB 16.3 KB | Display Display | ![]() |
Images | ![]() | 51.8 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 165.2 MB 165.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 723.4 KB | Display | ![]() |
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Full document | ![]() | 723 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 18.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9e68MC ![]() 9e62C ![]() 9e63C ![]() 9e64C ![]() 9e65C ![]() 9e66C ![]() 9e67C C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.86 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : MscS/YnaI chimera
Entire | Name: MscS/YnaI chimera |
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Components |
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-Supramolecule #1: MscS/YnaI chimera
Supramolecule | Name: MscS/YnaI chimera / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 240 KDa |
-Macromolecule #1: MscS/YnaI chimera
Macromolecule | Name: MscS/YnaI chimera / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 34.443734 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IDFICTSLIA VILTIKLFLL INQFEKQQIK KGRDITSARI MSRIIKITII VVLVLLYGE HFGMSLSGLL TFGGIGGLAV GMAGKDILSN FFSGIMLYFD RPFSIGDWIR SPDRNIEGTV AEIGWRITKI T TFDNRPLY ...String: MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IDFICTSLIA VILTIKLFLL INQFEKQQIK KGRDITSARI MSRIIKITII VVLVLLYGE HFGMSLSGLL TFGGIGGLAV GMAGKDILSN FFSGIMLYFD RPFSIGDWIR SPDRNIEGTV AEIGWRITKI T TFDNRPLY VPNSLFSSIS VENPGRMTNR RITTTIGLRY EDAAKVGVIV EAVREMLKNH PAIDQRQTLL VYFNQFADSS LN IMVYCFT KTTVWAEWLA AQQDVYLKII DIVQSHGADF AFPSQTLYMD NITPPEQGRA AALEHHHHHH UniProtKB: Small-conductance mechanosensitive channel, Low conductance mechanosensitive channel YnaI |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.5 sec. / Average electron dose: 54.76 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |