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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | cryo-EM structure of FtsE/X and ZipA complex in filament | |||||||||
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![]() | cell division / division filament / FtsE/X / ZipA / CELL CYCLE | |||||||||
Function / homology | ![]() division septum / divisome complex / Gram-negative-bacterium-type cell wall / signal recognition particle binding / peptidoglycan turnover / plasma membrane protein complex / SRP-dependent cotranslational protein targeting to membrane / division septum assembly / FtsZ-dependent cytokinesis / cell division site ...division septum / divisome complex / Gram-negative-bacterium-type cell wall / signal recognition particle binding / peptidoglycan turnover / plasma membrane protein complex / SRP-dependent cotranslational protein targeting to membrane / division septum assembly / FtsZ-dependent cytokinesis / cell division site / ATPase complex / positive regulation of cell division / cell division / GTPase activity / GTP binding / protein homodimerization activity / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Zhu KF / Li JW / Luo M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: cryo-EM structure of FtsE/X and ZipA complex in filament Authors: Zhu KF / Li JW / Luo M | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 483.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.3 KB 20.3 KB | Display Display | ![]() |
Images | ![]() | 163.4 KB | ||
Filedesc metadata | ![]() | 6.3 KB | ||
Others | ![]() ![]() | 462.2 MB 462.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 913.4 KB | Display | ![]() |
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Full document | ![]() | 913.1 KB | Display | |
Data in XML | ![]() | 18.9 KB | Display | |
Data in CIF | ![]() | 22.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9iueMC 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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
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_60898_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_60898_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : complex of FtsE/X-ZipA in filament
Entire | Name: complex of FtsE/X-ZipA in filament |
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Components |
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-Supramolecule #1: complex of FtsE/X-ZipA in filament
Supramolecule | Name: complex of FtsE/X-ZipA in filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Cell division protein ZipA
Macromolecule | Name: Cell division protein ZipA / type: protein_or_peptide / ID: 1 / Number of copies: 18 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 36.517199 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD EGVGEVRVHR VNHAPANAQE HEAARPSPQ HQYQPPYASA QPRQPVQQPP EAQVPPQHAP HPAQPVQQPA YQPQPEQPLQ QPVSPQVAPA PQPVHSAPQP A QQAFQPAE ...String: MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD EGVGEVRVHR VNHAPANAQE HEAARPSPQ HQYQPPYASA QPRQPVQQPP EAQVPPQHAP HPAQPVQQPA YQPQPEQPLQ QPVSPQVAPA PQPVHSAPQP A QQAFQPAE PVAAPQPEPV AEPAPVMDKP KRKEAVIIMN VAAHHGSELN GELLLNSIQQ AGFIFGDMNI YHRHLSPDGS GP ALFSLAN MVKPGTFDPE MKDFTTPGVT IFMQVPSYGD ELQNFKLMLQ SAQHIADEVG GVVLDDQRRM MTPQKLREYQ DII REVKDA NA UniProtKB: Cell division protein ZipA |
-Macromolecule #2: Cell division ATP-binding protein FtsE
Macromolecule | Name: Cell division ATP-binding protein FtsE / type: protein_or_peptide / ID: 2 / Number of copies: 18 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 24.832695 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SGLVMIRFEH VSKAYLGGRQ ALQGVTFHMQ PGEMAFLTGH SGAGKSTLLK LICGIERPSA GKIWFSGHDI TRLKNREVPF LRRQIGMIF QDHHLLMDRT VYDNVAIPLI IAGASGDDIR RRVSAALDKV GLLDKAKNFP IQLSGGEQQR VGIARAVVNK P AVLLADEP ...String: SGLVMIRFEH VSKAYLGGRQ ALQGVTFHMQ PGEMAFLTGH SGAGKSTLLK LICGIERPSA GKIWFSGHDI TRLKNREVPF LRRQIGMIF QDHHLLMDRT VYDNVAIPLI IAGASGDDIR RRVSAALDKV GLLDKAKNFP IQLSGGEQQR VGIARAVVNK P AVLLADEP TGNLDDALSE GILRLFEEFN RVGVTVLMAT HDINLISRRS YRMLTLSDGH LHGGVGHE UniProtKB: Cell division ATP-binding protein FtsE |
-Macromolecule #3: Cell division protein FtsX
Macromolecule | Name: Cell division protein FtsX / type: protein_or_peptide / ID: 3 / Number of copies: 18 / 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 #4: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 4 / Number of copies: 18 / Formula: AGS |
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Molecular weight | Theoretical: 523.247 Da |
Chemical component information | ![]() ChemComp-AGS: |
-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: NITROGEN |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #0 - Average electron dose: 40.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #1 - Average electron dose: 36.65 e/Å2 / #2 - Image recording ID: 3 / #2 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #2 - Average electron dose: 36.65 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: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |