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- EMDB-41100: CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming... -
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Open data
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Basic information
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Title | CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring from Salmonella | |||||||||
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![]() | Domain Swap / Symmetry mismatch / Flagellar component / Switch complex / MOTOR PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
![]() | Singh PK / Iverson TM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: CryoEM structures reveal how the bacterial flagellum rotates and switches direction. Authors: Prashant K Singh / Pankaj Sharma / Oshri Afanzar / Margo H Goldfarb / Elena Maklashina / Michael Eisenbach / Gary Cecchini / T M Iverson / ![]() ![]() Abstract: Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural ...Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 860.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.4 KB 19.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 28.6 KB | Display | ![]() |
Images | ![]() | 69 KB | ||
Masks | ![]() | 1.7 GB | ![]() | |
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() | 1.6 GB 1.6 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8t8oMC ![]() 8t8pC ![]() 8vibC ![]() 8vidC ![]() 8vkqC ![]() 8vkrC C: citing same article ( M: atomic model generated by this map |
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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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Voxel size | X=Y=Z: 1.363 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #1
File | emd_41100_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_41100_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM,...
Entire | Name: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM, and FliN |
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Components |
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-Supramolecule #1: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM,...
Supramolecule | Name: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM, and FliN type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 3.5 MDa |
-Macromolecule #1: Flagellar M-ring protein
Macromolecule | Name: Flagellar M-ring protein / type: protein_or_peptide / ID: 1 / Number of copies: 34 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 5.644328 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: KDEQLQQRRA NQRLGAEVMS QRIREMSDND PRVVALVIRQ WMSNDHE UniProtKB: Flagellar M-ring protein |
-Macromolecule #2: Flagellar motor switch protein FliG
Macromolecule | Name: Flagellar motor switch protein FliG / type: protein_or_peptide / ID: 2 / Number of copies: 34 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 36.890957 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSNLSGTDKS VILLMTIGED RAAEVFKHLS TREVQALSTA MANVRQISNK QLTDVLSEFE QEAEQFAALN INANEYLRSV LVKALGEER ASSLLEDILE TRDTTSGIET LNFMEPQSAA DLIRDEHPQI IATILVHLKR SQAADILALF DERLRHDVML R IATFGGVQ ...String: MSNLSGTDKS VILLMTIGED RAAEVFKHLS TREVQALSTA MANVRQISNK QLTDVLSEFE QEAEQFAALN INANEYLRSV LVKALGEER ASSLLEDILE TRDTTSGIET LNFMEPQSAA DLIRDEHPQI IATILVHLKR SQAADILALF DERLRHDVML R IATFGGVQ PAALAELTEV LNGLLDGQNL KRSKMGGVRT AAEIINLMKT QQEEAVITAV REFDGELAQK IIDEMFLFEN LV DVDDRSI QRLLQEVDSE SLLIALKGAE PPLREKFLRN MSQRAADILR DDLANRGPVR LSQVENEQKA ILLIVRRLAE TGE MVIGSG EDTYV UniProtKB: Flagellar motor switch protein FliG |
-Macromolecule #3: FliM,Flagellar motor switch protein FliM
Macromolecule | Name: FliM,Flagellar motor switch protein FliM / type: protein_or_peptide / ID: 3 / Number of copies: 34 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33.758836 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) LQA LEIINERFAR QFRMGLFNLL RRSPDITVGA IRIQPYHEFA RNLPVPTNLN LIHLKPLRGT GLVVFSPSLV FIAVDNL FG GDGRFPTKVE ...String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) LQA LEIINERFAR QFRMGLFNLL RRSPDITVGA IRIQPYHEFA RNLPVPTNLN LIHLKPLRGT GLVVFSPSLV FIAVDNL FG GDGRFPTKVE GREFTHTEQR VINRMLKLAL EGYSDAWKAI NPLEVEYVRS EMQVKFTNIT TSPNDIVVNT PFHVEIGN L TGEFNICLPF SMIEPLRELL VNPPLENSRH EDQNWRDNLV RQVQHSELEL VANFADIPLR LSQILKLKPG DVLPIEKPD RIIAHVDGVP VLTSQYGTVN GQYALRVEHL INPILNSLNE EQPK UniProtKB: Flagellar motor switch protein FliM |
-Macromolecule #4: Flagellar motor switch protein FliN
Macromolecule | Name: Flagellar motor switch protein FliN / type: protein_or_peptide / ID: 4 / Number of copies: 102 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 14.801823 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSDMNNPSDE NTGALDDLWA DALNEQKATT TKSAADAVFQ QLGGGDVSGA MQDIDLIMDI PVKLTVELGR TRMTIKELLR LTQGSVVAL DGLAGEPLDI LINGYLIAQG EVVVVADKYG VRITDIITPS ERMRRLSR UniProtKB: Flagellar motor switch protein FliN |
-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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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 51.557 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |