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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

Entry
Database: EMDB / ID: EMD-37325
TitleCryo-EM structure of Escherichia coli Str K12 FtsE(E163Q)X/EnvC complex with ATP in peptidisc
Map data
Sample
  • Complex: ATP bound FtsE(E163Q)X-EnvC complex
    • Protein or peptide: Cell division ATP-binding protein FtsE
    • Protein or peptide: Cell division protein FtsX
    • Protein or peptide: Murein hydrolase activator EnvC
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
Keywordscomplex / TRANSPORT PROTEIN
Function / homology
Function and homology information


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 / division septum assembly / FtsZ-dependent cytokinesis / 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 / division septum assembly / FtsZ-dependent cytokinesis / extrinsic component of membrane / cell division site / ATPase complex / positive regulation of cell division / transmembrane transporter activity / response to radiation / metalloendopeptidase activity / transmembrane transport / 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
: / Cell division protein FtsE, ATP-binding / Cell division protein FtsX / FtsX, extracellular domain / FtsX extracellular domain / : / ABC transporter, lipoprotein release, LolD / Peptidase M23 / Peptidase family M23 / Duplicated hybrid motif ...: / Cell division protein FtsE, ATP-binding / Cell division protein FtsX / FtsX, extracellular domain / FtsX extracellular domain / : / ABC transporter, lipoprotein release, LolD / Peptidase M23 / Peptidase family M23 / Duplicated hybrid motif / ABC3 transporter permease protein domain / FtsX-like permease C-terminal / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Cell division ATP-binding protein FtsE / Cell division protein FtsX / Murein hydrolase activator EnvC
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsLi J / Xu X / He Y / Luo M
Funding support Singapore, 1 items
OrganizationGrant numberCountry
Ministry of Education (MoE, Singapore)A-0008412-00-00 Singapore
CitationJournal: To Be Published
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
DepositionAug 29, 2023-
Header (metadata) releaseDec 20, 2023-
Map releaseDec 20, 2023-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_37325.png

Downloads & links

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Map

FileDownload / File: emd_37325.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 256 pix.
= 271.36 Å		1.06 Å/pix.
x 256 pix.
= 271.36 Å		1.06 Å/pix.
x 256 pix.
= 271.36 Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.09
Minimum - Maximum-0.9241503 - 1.5116667
Average (Standard dev.)0.0004288847 (±0.036003467)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 271.36 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_37325_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_37325_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : ATP bound FtsE(E163Q)X-EnvC complex

EntireName: ATP bound FtsE(E163Q)X-EnvC complex
Components
  • Complex: ATP bound FtsE(E163Q)X-EnvC complex
    • Protein or peptide: Cell division ATP-binding protein FtsE
    • Protein or peptide: Cell division protein FtsX
    • Protein or peptide: Murein hydrolase activator EnvC
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: ATP bound FtsE(E163Q)X-EnvC complex

SupramoleculeName: ATP bound FtsE(E163Q)X-EnvC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Escherichia coli K-12 (bacteria)

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Macromolecule #1: Cell division ATP-binding protein FtsE

MacromoleculeName: Cell division ATP-binding protein FtsE / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 24.475295 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: 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

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Macromolecule #2: Cell division protein FtsX

MacromoleculeName: Cell division protein FtsX / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 38.5835 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: 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

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Macromolecule #3: Murein hydrolase activator EnvC

MacromoleculeName: Murein hydrolase activator EnvC / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 46.661617 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: 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

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Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 2 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm 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 beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 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

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 182732
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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