+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-10828 | |||||||||
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Title | Structure of C. jejuni MotAB | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Bacterial flagellar motor / stator unit / locomotion / proton transport / ion transport / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information bacterial-type flagellum-dependent swarming motility / chemotaxis / plasma membrane Similarity search - Function | |||||||||
Biological species | Campylobacter jejuni subsp. jejuni 81-176 (Campylobacter) / Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) (Campylobacter) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Santiveri M / Roa-Eguiara A | |||||||||
Funding support | Denmark, 2 items
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Citation | Journal: Cell / Year: 2020 Title: Structure and Function of Stator Units of the Bacterial Flagellar Motor. Authors: Mònica Santiveri / Aritz Roa-Eguiara / Caroline Kühne / Navish Wadhwa / Haidai Hu / Howard C Berg / Marc Erhardt / Nicholas M I Taylor / Abstract: Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate ...Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate torque at the interface between stator units and rotor. The structural organization of the stator unit (MotAB), its conformational changes upon ion transport, and how these changes power rotation of the flagellum remain unknown. Here, we present ~3 Å-resolution cryoelectron microscopy reconstructions of the stator unit in different functional states. We show that the stator unit consists of a dimer of MotB surrounded by a pentamer of MotA. Combining structural data with mutagenesis and functional studies, we identify key residues involved in torque generation and present a detailed mechanistic model for motor function and switching of rotational direction. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_10828.map.gz | 6.7 MB | EMDB map data format | |
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Header (meta data) | emd-10828-v30.xml emd-10828.xml | 16 KB 16 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_10828_fsc.xml | 9.2 KB | Display | FSC data file |
Images | emd_10828.png | 119.3 KB | ||
Masks | emd_10828_msk_1.map | 64 MB | Mask map | |
Filedesc metadata | emd-10828.cif.gz | 5.7 KB | ||
Others | emd_10828_half_map_1.map.gz emd_10828_half_map_2.map.gz | 49.4 MB 49.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-10828 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-10828 | HTTPS FTP |
-Validation report
Summary document | emd_10828_validation.pdf.gz | 189.6 KB | Display | EMDB validaton report |
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Full document | emd_10828_full_validation.pdf.gz | 189.2 KB | Display | |
Data in XML | emd_10828_validation.xml.gz | 503 B | Display | |
Data in CIF | emd_10828_validation.cif.gz | 373 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10828 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10828 | HTTPS FTP |
-Related structure data
Related structure data | 6ykmMC 6ykpC 6ykrC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_10828.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_10828_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_10828_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_10828_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Stator unit MotAB
Entire | Name: Stator unit MotAB |
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Components |
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-Supramolecule #1: Stator unit MotAB
Supramolecule | Name: Stator unit MotAB / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: The stator unit consists of a dimer of MotB surrounded by a pentamer of MotA |
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Source (natural) | Organism: Campylobacter jejuni subsp. jejuni 81-176 (Campylobacter) |
-Macromolecule #1: Chemotaxis protein MotA, putative
Macromolecule | Name: Chemotaxis protein MotA, putative / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) (Campylobacter) Strain: 81-176 |
Molecular weight | Theoretical: 28.195816 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MDLSTILGMV LAVTSISVGD ILEGGNPLHV IHLSSFLIVM PTAAFCAMTS THKKIVKAAY KELKVVFKGS GVNLPERIAQ LIEFAIIAR RDGLLALESR TNEIENEFLK NAMMMLVDGK SFEEIHESME IQTEQLEEHY KECAEYWIVF GETCPTMGLV G AVFGLILA ...String: MDLSTILGMV LAVTSISVGD ILEGGNPLHV IHLSSFLIVM PTAAFCAMTS THKKIVKAAY KELKVVFKGS GVNLPERIAQ LIEFAIIAR RDGLLALESR TNEIENEFLK NAMMMLVDGK SFEEIHESME IQTEQLEEHY KECAEYWIVF GETCPTMGLV G AVFGLILA LKLLDNPQAM AAGISGAFTA TVTGIFGAYA LFAPWGKKLK ANGMDLVKEQ IVITEAIKGI AEGANPRDLE AK LFNFLSH DDPRISQFDK G UniProtKB: Chemotaxis protein MotA, putative |
-Macromolecule #2: Chemotaxis protein MotB, putative
Macromolecule | Name: Chemotaxis protein MotB, putative / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) (Campylobacter) Strain: 81-176 |
Molecular weight | Theoretical: 32.149244 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MAKKHKCPEC PAGEKWAVPY ADFLSLLLAL FIALWAISKT NPAKVEALKT EFVKIFDYTS TQTVKEESKT QEKYKGAAKE ESDELKSLK QMTMTQQETI KRLQAALDQS DNQVALNLPS KVEFERGSAQ IVSADIQDYL KRMAELTTYL PPQAKIEIRG Y TDNSDSII ...String: MAKKHKCPEC PAGEKWAVPY ADFLSLLLAL FIALWAISKT NPAKVEALKT EFVKIFDYTS TQTVKEESKT QEKYKGAAKE ESDELKSLK QMTMTQQETI KRLQAALDQS DNQVALNLPS KVEFERGSAQ IVSADIQDYL KRMAELTTYL PPQAKIEIRG Y TDNSDSII RSYELAYQRA ENVLKYFIEG GANLKNISIK SYGLNNPING NPQALENNRV EIYFKVDTAD TSTQKSVLEL IN KIGTKAP GTLEVLFQGP GGSGSAWSHP QFEKGGGSGG GSGGSAWSHP QFEK UniProtKB: Chemotaxis protein MotB, putative |
-Macromolecule #3: water
Macromolecule | Name: water / type: ligand / ID: 3 / Number of copies: 8 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.65 mg/mL |
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Buffer | pH: 8 |
Grid | Model: Quantifoil R2/1 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 40.84 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |