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- EMDB-41763: Cryo-EM structure of Vibrio cholerae FtsE Y20A mutant/FtsX/EnvC c... -
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Open data
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Basic information
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Title | Cryo-EM structure of Vibrio cholerae FtsE Y20A mutant/FtsX/EnvC complex | |||||||||
![]() | full map_updated | |||||||||
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![]() | membrane protein / enzyme / TRANSPORT PROTEIN | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.37 Å | |||||||||
![]() | Hao A / Lee S-Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the FtsEX-EnvC complex regulation on septal peptidoglycan hydrolysis in Vibrio cholerae. Authors: Aili Hao / Yang Suo / Seok-Yong Lee / ![]() Abstract: During bacterial cell division, hydrolysis of septal peptidoglycan (sPG) is crucial for cell separation. This sPG hydrolysis is performed by the enzyme amidases whose activity is regulated by the ...During bacterial cell division, hydrolysis of septal peptidoglycan (sPG) is crucial for cell separation. This sPG hydrolysis is performed by the enzyme amidases whose activity is regulated by the integral membrane protein complex FtsEX-EnvC. FtsEX is an ATP-binding cassette transporter, and EnvC is a long coiled-coil protein that interacts with and activates the amidases. The molecular mechanism by which the FtsEX-EnvC complex activates amidases remains largely unclear. We present the cryo-electron microscopy structure of the FtsEX-EnvC complex from the pathogenic bacteria V. cholerae (FtsEX-EnvC). FtsEX-EnvC in the presence of ADP adopts a distinct conformation where EnvC is "horizontally extended" rather than "vertically extended". Subsequent structural studies suggest that EnvC can swing between these conformations in space in a nucleotide-dependent manner. Our structural analysis and functional studies suggest that FtsEX-EnvC employs spatial control of EnvC for amidase activation, providing mechanistic insights into the FtsEX-EnvC regulation on septal peptidoglycan hydrolysis. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 251.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.5 KB 16.5 KB | Display Display | ![]() |
Images | ![]() | 38.8 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() | 474.9 MB 475 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 717.9 KB | Display | ![]() |
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Full document | ![]() | 717.4 KB | Display | |
Data in XML | ![]() | 18.9 KB | Display | |
Data in CIF | ![]() | 22.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | full map_updated | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: half map B updated
File | emd_41763_half_map_1.map | ||||||||||||
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Annotation | half map B_updated | ||||||||||||
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Density Histograms |
-Half map: half map A updated
File | emd_41763_half_map_2.map | ||||||||||||
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Annotation | half map A_updated | ||||||||||||
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Density Histograms |
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Sample components
-Entire : FtsEX
Entire | Name: FtsEX |
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Components |
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-Supramolecule #1: FtsEX
Supramolecule | Name: FtsEX / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 200 KDa |
-Macromolecule #1: FtsE
Macromolecule | Name: FtsE / type: protein_or_peptide / ID: 1 / Enantiomer: DEXTRO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: PALSGGDGVI RFQQVSKAYR GGRQALQKVD FHLRRGEMAF LGGHSGAGKS TLLKLICAIE RPTDGKISFN GHDITRIPNK DIPFLRRNIG IVFQDHRLLM DRSIYDNVAL PMRIESISEN EIKRRVSAAL DKTGLLDKAR CLPSQLSGGE QQRVGIARAV VNRPTLLLAD ...String: PALSGGDGVI RFQQVSKAYR GGRQALQKVD FHLRRGEMAF LGGHSGAGKS TLLKLICAIE RPTDGKISFN GHDITRIPNK DIPFLRRNIG IVFQDHRLLM DRSIYDNVAL PMRIESISEN EIKRRVSAAL DKTGLLDKAR CLPSQLSGGE QQRVGIARAV VNRPTLLLAD EPTGNLDPEL SSRVLRLFEE FNRAGVTILL ATHDIHLVNS RPQYRHLELN QGFLSEVADY GR |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 8 mg/mL | |||||||||
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Buffer | pH: 8 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Average exposure time: 2.4 sec. / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT |