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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | E. coli TolAQR conformation I | |||||||||
![]() | TolAtevQR-I in LMNG | |||||||||
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![]() | Tol-Pal system / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() cellular response to bacteriocin / cell septum assembly / regulation of membrane invagination / bacteriocin transport / toxin transmembrane transporter activity / protein import / virion binding / cell division site / transmembrane transporter activity / disordered domain specific binding ...cellular response to bacteriocin / cell septum assembly / regulation of membrane invagination / bacteriocin transport / toxin transmembrane transporter activity / protein import / virion binding / cell division site / transmembrane transporter activity / disordered domain specific binding / protein transport / protein domain specific binding / symbiont entry into host cell / cell division / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.94 Å | |||||||||
![]() | Celia H / Botos I | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of the E. coli Ton and Tol motor complexes Authors: Celia H / Botos I / Ghirlando R / Duche D / Beach BM / Lloubes R / Buchanan SK | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 32.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.4 KB 17.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.5 KB | Display | ![]() |
Images | ![]() | 174 KB | ||
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() | 59.5 MB 59.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 16.3 KB | Display | |
Data in CIF | ![]() | 21.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ddmMC ![]() 9ddnC ![]() 9ddoC ![]() 9ddpC ![]() 9ddqC 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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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | TolAtevQR-I in LMNG | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: halfmap A
File | emd_46776_half_map_1.map | ||||||||||||
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Annotation | halfmap A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: halfmap B
File | emd_46776_half_map_2.map | ||||||||||||
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Annotation | halfmap B | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : TolAQR complex
Entire | Name: TolAQR complex |
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Components |
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-Supramolecule #1: TolAQR complex
Supramolecule | Name: TolAQR complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Tol-Pal system protein TolQ
Macromolecule | Name: Tol-Pal system protein TolQ / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 25.623662 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTDMNILDLF LKASLLVKLI MLILIGFSIA SWAIIIQRTR ILNAAAREAE AFEDKFWSGI ELSRLYQESQ GKRDNLTGSE QIFYSGFKE FVRLHRANSH APEAVVEGAS RAMRISMNRE LENLETHIPF LGTVGSISPY IGLFGTVWGI MHAFIALGAV K QATLQMVA ...String: MTDMNILDLF LKASLLVKLI MLILIGFSIA SWAIIIQRTR ILNAAAREAE AFEDKFWSGI ELSRLYQESQ GKRDNLTGSE QIFYSGFKE FVRLHRANSH APEAVVEGAS RAMRISMNRE LENLETHIPF LGTVGSISPY IGLFGTVWGI MHAFIALGAV K QATLQMVA PGIAEALIAT AIGLFAAIPA VMAYNRLNQR VNKLELNYDN FMEEFTAILH RQAFTVSESN KG UniProtKB: Tol-Pal system protein TolQ |
-Macromolecule #2: Tol-Pal system protein TolA
Macromolecule | Name: Tol-Pal system protein TolA / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 44.563109 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGSWSHPQFE KGSSKATEQN DKLKRAIIIS AVLHVILFAA LIWSSFDENI EASAGGGGGS SIDAVMVDSG AVVEQYKRMQ SQESSAKRS DEQRKMKEQQ AAEELREKQA AEQERLKQLE KERLAAQEQK KQAEEAAKQA ELKQKQAEEA AAKAAADAKA K AEADAKAA ...String: MGSWSHPQFE KGSSKATEQN DKLKRAIIIS AVLHVILFAA LIWSSFDENI EASAGGGGGS SIDAVMVDSG AVVEQYKRMQ SQESSAKRS DEQRKMKEQQ AAEELREKQA AEQERLKQLE KERLAAQEQK KQAEEAAKQA ELKQKQAEEA AAKAAADAKA K AEADAKAA EEAAKKAAAD AKKKAEAEAA KAAAEAQKKA EAAAAALKKK AEAAEAAAAE ARKKAATEAA EKAKAEAEKK AA AEKAAAD KKAAAEKAAA DKKAAEKAAA EKAAADKKAA AEKAAADKKA AAAKAAAEKA AAAKAAAEAD DIFGELSSGK NAP KTGGGA KGNNASPAGS GNTKNNGASG ADINNYAGQI KSAIESKFYD ASSYAGKTCT LRIKLAPDGM LLDIKPEGGD PALC QAALA AAKLAKIPKP PSQAVYEVFK NAPLDFKP UniProtKB: Tol-Pal system protein TolA |
-Macromolecule #3: Tol-Pal system protein TolR
Macromolecule | Name: Tol-Pal system protein TolR / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 15.398884 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MARARGRGRR DLKSEINIVP LLDVLLVLLL IFMATAPIIT QSVEVDLPDA TESQAVSSND NPPVIVEVSG IGQYTVVVEK DRLERLPPE QVVAEVSSRF KANPKTVFLI GGAKDVPYDE IIKALNLLHS AGVKSVGLMT QPI UniProtKB: Tol-Pal system protein TolR |
-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: 7.5 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 61.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm |
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
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | ![]() PDB-9ddm: |