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- EMDB-37325: Cryo-EM structure of Escherichia coli Str K12 FtsE(E163Q)X/EnvC c... -
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Basic information
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Title | Cryo-EM structure of Escherichia coli Str K12 FtsE(E163Q)X/EnvC complex with ATP in peptidisc | |||||||||
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![]() | complex / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() division septum / divisome complex / peptidoglycan-based cell wall biogenesis / Gram-negative-bacterium-type cell wall / septum digestion after cytokinesis / peptidoglycan turnover / plasma membrane protein complex / FtsZ-dependent cytokinesis / division septum assembly / extrinsic component of membrane ...division septum / divisome complex / peptidoglycan-based cell wall biogenesis / Gram-negative-bacterium-type cell wall / septum digestion after cytokinesis / peptidoglycan turnover / plasma membrane protein complex / FtsZ-dependent cytokinesis / division septum assembly / extrinsic component of membrane / ATPase complex / cell division site / positive regulation of cell division / transmembrane transporter activity / response to radiation / transmembrane transport / metalloendopeptidase activity / outer membrane-bounded periplasmic space / periplasmic space / hydrolase activity / response to xenobiotic stimulus / cell division / response to antibiotic / ATP hydrolysis activity / ATP binding / membrane / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
![]() | Li J / Xu X / He Y / Luo M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of Escherichia coli Str K12 FtsE(E163Q)X/EnvC complex with ATP in peptidisc Authors: Li J / Xu X / He Y / Luo M | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.2 KB 16.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.4 KB | Display | ![]() |
Images | ![]() | 31.4 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 59.3 MB 59.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8w6jMC M: atomic model generated by this map C: citing same article ( |
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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: 1.06 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_37325_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_37325_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : ATP bound FtsE(E163Q)X-EnvC complex
Entire | Name: ATP bound FtsE(E163Q)X-EnvC complex |
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Components |
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-Supramolecule #1: ATP bound FtsE(E163Q)X-EnvC complex
Supramolecule | Name: ATP bound FtsE(E163Q)X-EnvC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() ![]() |
-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: 24.475295 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MIRFEHVSKA YLGGRQALQG VTFHMQPGEM AFLTGHSGAG KSTLLKLICG IERPSAGKIW FSGHDITRLK NREVPFLRRQ IGMIFQDHH LLMDRTVYDN VAIPLIIAGA SGDDIRRRVS AALDKVGLLD KAKNFPIQLS GGEQQRVGIA RAVVNKPAVL L ADQPTGNL ...String: MIRFEHVSKA YLGGRQALQG VTFHMQPGEM AFLTGHSGAG KSTLLKLICG IERPSAGKIW FSGHDITRLK NREVPFLRRQ IGMIFQDHH LLMDRTVYDN VAIPLIIAGA SGDDIRRRVS AALDKVGLLD KAKNFPIQLS GGEQQRVGIA RAVVNKPAVL L ADQPTGNL DDALSEGILR LFEEFNRVGV TVLMATHDIN LISRRSYRML TLSDGHLHGG VGHE 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: 38.5835 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNKRDAINHI RQFGGRLDRF RKSVGGSGDG GRNAPKRAKS SPKPVNRKTN VFNEQVRYAF HGALQDLKSK PFATFLTVMV IAISLTLPS VCYMVYKNVN QAATQYYPSP QITVYLQKTL DDDAAAGVVA QLQAEQGVEK VNYLSREDAL GEFRNWSGFG G ALDMLEEN ...String: MNKRDAINHI RQFGGRLDRF RKSVGGSGDG GRNAPKRAKS SPKPVNRKTN VFNEQVRYAF HGALQDLKSK PFATFLTVMV IAISLTLPS VCYMVYKNVN QAATQYYPSP QITVYLQKTL DDDAAAGVVA QLQAEQGVEK VNYLSREDAL GEFRNWSGFG G ALDMLEEN PLPAVAVVIP KLDFQGTESL NTLRDRITQI NGIDEVRMDD SWFARLAALT GLVGRVSAMI GVLMVAAVFL VI GNSVRLS IFARRDSINV QKLIGATDGF ILRPFLYGGA LLGFSGALLS LILSEILVLR LSSAVAEVAQ VFGTKFDING LSF DECLLL LLVCSMIGWV AAWLATVQHL RHFTPE UniProtKB: Cell division protein FtsX |
-Macromolecule #3: Murein hydrolase activator EnvC
Macromolecule | Name: Murein hydrolase activator EnvC / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 46.661617 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTRAVKPRRF AIRPIIYASV LSAGVLLCAF SAHADERDQL KSIQADIAAK ERAVRQKQQQ RASLLAQLKK QEEAISEATR KLRETQNTL NQLNKQIDEM NASIAKLEQQ KAAQERSLAA QLDAAFRQGE HTGIQLILSG EESQRGQRLQ AYFGYLNQAR Q ETIAQLKQ ...String: MTRAVKPRRF AIRPIIYASV LSAGVLLCAF SAHADERDQL KSIQADIAAK ERAVRQKQQQ RASLLAQLKK QEEAISEATR KLRETQNTL NQLNKQIDEM NASIAKLEQQ KAAQERSLAA QLDAAFRQGE HTGIQLILSG EESQRGQRLQ AYFGYLNQAR Q ETIAQLKQ TREEVAMQRA ELEEKQSEQQ TLLYEQRAQQ AKLTQALNER KKTLAGLESS IQQGQQQLSE LRANESRLRN SI ARAEAAA KARAEREARE AQAVRDRQKE ATRKGTTYKP TESEKSLMSR TGGLGAPRGQ AFWPVRGPTL HRYGEQLQGE LRW KGMVIG ASEGTEVKAI ADGRVILADW LQGYGLVVVV EHGKGDMSLY GYNQSALVSV GSQVRAGQPI ALVGSSGGQG RPSL YFEIR RQGQAVNPQP WLGR UniProtKB: Murein hydrolase activator EnvC |
-Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 2 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-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: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Average exposure time: 6.02 sec. / Average electron dose: 38.837 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 2.5 µm / Calibrated defocus min: 1.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |