+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-42139 | |||||||||
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Title | Cryo-EM structure of the flagellar MotAB stator bound to FliG | |||||||||
Map data | Global B-factor sharpened map | |||||||||
Sample |
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Keywords | flagella chemotaxis motility type III secretion system / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | |||||||||
Biological species | Clostridium sporogenes (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.4 Å | |||||||||
Authors | Deme JC / Johnson S / Lea SM | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Nat Microbiol / Year: 2024 Title: Structural basis of directional switching by the bacterial flagellum. Authors: Steven Johnson / Justin C Deme / Emily J Furlong / Joseph J E Caesar / Fabienne F V Chevance / Kelly T Hughes / Susan M Lea / Abstract: The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar ...The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar filament. Rotation is bi-directional, with binding of a cytoplasmic chemotactic response regulator controlling reversal, though the structural and mechanistic bases for rotational switching are not well understood. Here we present cryoelectron microscopy structures of intact Salmonella flagellar basal bodies (3.2-5.5 Å), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180° movements of both the N- and C-terminal domains of the FliG protein, which, when combined with a high-resolution cryoelectron microscopy structure of the MotAB stator, show that the stator shifts from the outside to the inside of the C-ring. This enables rotational switching and reveals how uni-directional ion flow across the inner membrane is used to accomplish bi-directional rotation of the flagellum. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_42139.map.gz | 323.7 MB | EMDB map data format | |
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Header (meta data) | emd-42139-v30.xml emd-42139.xml | 20.3 KB 20.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_42139_fsc.xml | 14.8 KB | Display | FSC data file |
Images | emd_42139.png | 159.6 KB | ||
Masks | emd_42139_msk_1.map | 343 MB | Mask map | |
Filedesc metadata | emd-42139.cif.gz | 6 KB | ||
Others | emd_42139_additional_1.map.gz emd_42139_additional_2.map.gz emd_42139_half_map_1.map.gz emd_42139_half_map_2.map.gz | 172.4 MB 283.6 MB 318.5 MB 318.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42139 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42139 | HTTPS FTP |
-Related structure data
Related structure data | 8ucsMC 8umdC 8umxC 8uoxC 8uplC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_42139.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Global B-factor sharpened map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.693 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_42139_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: unsharpened map
File | emd_42139_additional_1.map | ||||||||||||
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Annotation | unsharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Sharpened with deepEMhancer
File | emd_42139_additional_2.map | ||||||||||||
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Annotation | Sharpened with deepEMhancer | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 2
File | emd_42139_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 1
File | emd_42139_half_map_2.map | ||||||||||||
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Annotation | half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : MotAB stator complexed with FliG
Entire | Name: MotAB stator complexed with FliG |
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Components |
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-Supramolecule #1: MotAB stator complexed with FliG
Supramolecule | Name: MotAB stator complexed with FliG / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: Clostridium sporogenes (bacteria) |
-Macromolecule #1: OmpA family protein
Macromolecule | Name: OmpA family protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Clostridium sporogenes (bacteria) |
Molecular weight | Theoretical: 32.078861 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MARRNKKGGG GDEIRGDEWL ATFSDTITLL LTFFILLYSF SSVDAQKFQQ VASAMQVAMT GQSGNTIVDY NLKNGDVPLV GETTKLGRE TGSDAKSDSK EVYNEVNKFV DKNNLKSSVE VKEDGRGVII QLRDNVLFEI GRADIKPQSK QIMDKINGLI A TLPNEVIV ...String: MARRNKKGGG GDEIRGDEWL ATFSDTITLL LTFFILLYSF SSVDAQKFQQ VASAMQVAMT GQSGNTIVDY NLKNGDVPLV GETTKLGRE TGSDAKSDSK EVYNEVNKFV DKNNLKSSVE VKEDGRGVII QLRDNVLFEI GRADIKPQSK QIMDKINGLI A TLPNEVIV EGHTDNVPIK NEVYGSNWEL STARAVNVLR YFVETKKQNP VRFTAAGYGE YRPIAQNNSD VNKAKNRRVN IV IVSKEKE SSKKENLYFQ GQFGSWSHPQ FEKGGGSGGG SGGGSWSHPQ FEK UniProtKB: OmpA family protein |
-Macromolecule #2: Motility protein A
Macromolecule | Name: Motility protein A / type: protein_or_peptide / ID: 2 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Clostridium sporogenes (bacteria) |
Molecular weight | Theoretical: 28.92885 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MKKRDILTPI GFVLCFGLVL WGMASGGSNL KVFWDVASVF ITIGGSMAAM LITYPMDEFK RLLIVIRQTF KDNGMSNIDV IQNFVDLSR KARREGLLSL EDAINNLTDD YMKKGLRMVV DGIEPETIRE IMELEIDEME KRHKSGADML KTWGGYAPAF G MVGTLIGL ...String: MKKRDILTPI GFVLCFGLVL WGMASGGSNL KVFWDVASVF ITIGGSMAAM LITYPMDEFK RLLIVIRQTF KDNGMSNIDV IQNFVDLSR KARREGLLSL EDAINNLTDD YMKKGLRMVV DGIEPETIRE IMELEIDEME KRHKSGADML KTWGGYAPAF G MVGTLIGL IQMLANLTDS STIASGMGKA LITTFYGSLM ANAVFNPMGA NLMFKSGVEA TTREMVLEGV LAIQSGVNPR IM EEKLVSY LSPPERQAYS KVQVS UniProtKB: Motility protein A |
-Macromolecule #3: Flagellar motor switch protein FliG
Macromolecule | Name: Flagellar motor switch protein FliG / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Clostridium sporogenes (bacteria) |
Molecular weight | Theoretical: 11.311659 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GGGSGGGSGG GSVFEDIITL DDVAIQRVLR EVETKDLALA LKGSSEEVAN VIFRNQSKRA ASSLKEDIEF LGPVRIMDVE KAQQGIVSI IRRLDEAGEI VISRGGED UniProtKB: Flagellar motor switch protein FliG |
-Macromolecule #4: water
Macromolecule | Name: water / type: ligand / ID: 4 / Number of copies: 2 / 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
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 56.5 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |