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- EMDB-41761: Cryo-EM structure of Vibrio cholerae FtsE/FtsX/EnvC complex, shortened -
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Open data
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Basic information
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Title | Cryo-EM structure of Vibrio cholerae FtsE/FtsX/EnvC complex, shortened | |||||||||
![]() | full map | |||||||||
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![]() | membrane protein / enzyme / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() septum digestion after cytokinesis / cell division site / transmembrane transporter activity / metalloendopeptidase activity / cell division / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.55 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 | ![]() | 179.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21 KB 21 KB | Display Display | ![]() |
Images | ![]() | 80.1 KB | ||
Masks | ![]() | 347.6 MB | ![]() | |
Filedesc metadata | ![]() | 6.9 KB | ||
Others | ![]() ![]() | 323 MB 323.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8tzkMC ![]() 8tzjC ![]() 8tzlC 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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Annotation | full map | ||||||||||||||||||||
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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-Half map: half map 2
File | emd_41761_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
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Density Histograms |
-Half map: half map 1
File | emd_41761_half_map_2.map | ||||||||||||
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Annotation | half map 1 | ||||||||||||
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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: #1-#3 |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 200 KDa |
-Macromolecule #1: Cell division ATP-binding protein FtsE
Macromolecule | Name: Cell division ATP-binding protein FtsE / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 25.882668 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: PALSGGDGVI RFQQVSKAYR GGRQALQKVD FHLRRGEMAF LGGHSGAGKS TLLKLICAIE RPTDGKISFN GHDITRIPNK DIPFLRRNI GIVFQDHRLL MDRSIYDNVA LPMRIESISE NEIKRRVSAA LDKTGLLDKA RCLPSQLSGG EQQRVGIARA V VNRPTLLL ...String: PALSGGDGVI RFQQVSKAYR GGRQALQKVD FHLRRGEMAF LGGHSGAGKS TLLKLICAIE RPTDGKISFN GHDITRIPNK DIPFLRRNI GIVFQDHRLL MDRSIYDNVA LPMRIESISE NEIKRRVSAA LDKTGLLDKA RCLPSQLSGG EQQRVGIARA V VNRPTLLL ADEPTGNLDP ELSSRVLRLF EEFNRAGVTI LLATHDIHLV NSRPQYRHLE LNQGFLSEVA DYGR UniProtKB: Cell division ATP-binding protein FtsE |
-Macromolecule #2: Cell division protein FtsX
Macromolecule | Name: Cell division protein FtsX / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 36.516773 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAVKPGNQKI SKTTKSTKSK PRDVKRAKTD SFLAIHFKQA KASFAALWRR PLGNILTLAV ISMALALPAS LYLLSKNIAS VAERVAEPS QLSVYLHIDT PEPRIIVLKD DLERRDEIAK VKYISPQQGL DDLSQYAGFE QAISLLDNAT LPAVLVVTPK V DSREQIQT ...String: MAVKPGNQKI SKTTKSTKSK PRDVKRAKTD SFLAIHFKQA KASFAALWRR PLGNILTLAV ISMALALPAS LYLLSKNIAS VAERVAEPS QLSVYLHIDT PEPRIIVLKD DLERRDEIAK VKYISPQQGL DDLSQYAGFE QAISLLDNAT LPAVLVVTPK V DSREQIQT LAKALQAEEG VTDVRMDEDW FARLDAIRHL ATIVVISLSS LMLMSVFLIV GNTLRFNVQA NKEEIQTMKL IG ATDAYIL RPYLYSGMWF GLLGAVAAWL LTALMTILLN GAVEALAQLY DSRFRLIGLG WDESLLLLML GVFLGCVAAK VSA KRHLKE IEPV UniProtKB: Cell division protein FtsX |
-Macromolecule #3: Peptidase M23
Macromolecule | Name: Peptidase M23 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 43.410895 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTATDPHAIF SDFLGKTLTH RLLACLLFMV SPSLFAATQQ ELTGVKSEIS RQQQSLAEQQ KSLDQLQQAL KQQELGINSI ENQITKTKN DLENANRNIA QLNSNIQALE TQKQQQADKL ERLLQTYYLT KRSLTNGQFF HRSADEDRIS QYYQHLAKSR A QAIEALEK ...String: MTATDPHAIF SDFLGKTLTH RLLACLLFMV SPSLFAATQQ ELTGVKSEIS RQQQSLAEQQ KSLDQLQQAL KQQELGINSI ENQITKTKN DLENANRNIA QLNSNIQALE TQKQQQADKL ERLLQTYYLT KRSLTNGQFF HRSADEDRIS QYYQHLAKSR A QAIEALEK TQTELNSNQK QRQTEREQIE KLLAEQTQQR DKLAKTQSER KQTVKKIESS ISGNKTYLAE LQRNETRLKA EI AKAAKRN AVLMNGIASQ RGKLPWPLKG RVLHNFGERQ TGQIDWKGLV IDANYGQEVK AVYPGTIVFA EYLRGYGLVV LLD HGKGDM TLYGFNQTLL KKEGDKVTTG ETIALAGDTG GQSRPALYFE IRRNSRAENP SQWLQR UniProtKB: Peptidase M23 |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 2 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-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 |
Output model | ![]() PDB-8tzk: |