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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | structure of FliD-FliC at a 10:10 stoichiometry | |||||||||
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![]() | Complex / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() TLR5 cascade / MyD88 cascade initiated on plasma membrane / bacterial-type flagellum filament cap / NFkB and MAPK activation mediated by TRAF6 / bacterial-type flagellum hook / The IPAF inflammasome / bacterial-type flagellum / bacterial-type flagellum-dependent cell motility / cell adhesion / receptor ligand activity ...TLR5 cascade / MyD88 cascade initiated on plasma membrane / bacterial-type flagellum filament cap / NFkB and MAPK activation mediated by TRAF6 / bacterial-type flagellum hook / The IPAF inflammasome / bacterial-type flagellum / bacterial-type flagellum-dependent cell motility / cell adhesion / receptor ligand activity / structural molecule activity / extracellular space / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.27 Å | |||||||||
![]() | Chen LX / Chen XQ / Zhang FF / Jiang WX / Xing Q | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the initiation of bacterial flagellar filament elongation Authors: Chen LX / Dong X / Zhang FF / Cheng XQ / Wang X / Jiang WX / Ma LX / Xing Q | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 778.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.7 KB 16.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 19.9 KB | Display | ![]() |
Images | ![]() | 89.7 KB | ||
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() | 765.6 MB 765.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 790.4 KB | Display | ![]() |
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Full document | ![]() | 790 KB | Display | |
Data in XML | ![]() | 29.7 KB | Display | |
Data in CIF | ![]() | 39.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9m6hMC 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: 0.75556 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_63662_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_63662_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : the FliD-FliC with 10:10 stoichiometry
Entire | Name: the FliD-FliC with 10:10 stoichiometry |
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Components |
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-Supramolecule #1: the FliD-FliC with 10:10 stoichiometry
Supramolecule | Name: the FliD-FliC with 10:10 stoichiometry / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Flagellar hook-associated protein 2
Macromolecule | Name: Flagellar hook-associated protein 2 / type: protein_or_peptide / ID: 1 Details: Sequence reference for strain 'Salmonella enterica subsp. enterica serovar Typhimurium' is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt id P16328. Number of copies: 10 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 45.971234 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: DLTKNEKGRL TPITKQQSAN SAKLTAYGTL KSALEKFQTA NTALNKADLF KSTVASSTTE DLKVSTTAGA AAGTYKINVT QLAAAQSLA TKTTFATTKE QLGDTSVTSR TIKIEQPGRK EPLEIKLDKG DTSMEAIRDA INDADSGIAA SIVKVKENEF Q LVLTANSG ...String: DLTKNEKGRL TPITKQQSAN SAKLTAYGTL KSALEKFQTA NTALNKADLF KSTVASSTTE DLKVSTTAGA AAGTYKINVT QLAAAQSLA TKTTFATTKE QLGDTSVTSR TIKIEQPGRK EPLEIKLDKG DTSMEAIRDA INDADSGIAA SIVKVKENEF Q LVLTANSG TDNTMKITVE GDTKLNDLLA YDSTTNTGNM QELVKAENAK LNVNGIDIER QSNTVTDAPQ GITLTLTKKV TD ATVTVTK DDTKAKEAIK SWVDAYNSLV DTFSSLTKYT AVEPGEEASD KNGALLGDSV VRTIQTGIRA QFANSGSNSA FKT MAEIGI TQDGTSGKLK IDDDKLTKVL KDNTAAAREL LVGDGKETGI TTKIATEVKS YLADDGIIDN AQDNVNATLK SLTK QYLSV SNSIDETVAR YKAQFTQLDT MMSKL UniProtKB: Flagellar hook-associated protein 2 |
-Macromolecule #2: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 2 Details: Sequence reference for strain 'Salmonella enterica subsp. enterica serovar Typhimurium' is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt id P06179. Number of copies: 10 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.695375 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: FTANIKGLTQ ASRNANDGIS IAQTTEGALN EINNNLQRVR ELAVQSANST NSQSDLDSIQ AEITQRLNEI DRVSGQTQFN GVKVLAQDN TLTIQVGAND GETIDIDLKQ INSQTLGLDT LNVQQKYKVS DTAATVTGYA DTTIALDNST FKASATGLGG T DQKIDGDL ...String: FTANIKGLTQ ASRNANDGIS IAQTTEGALN EINNNLQRVR ELAVQSANST NSQSDLDSIQ AEITQRLNEI DRVSGQTQFN GVKVLAQDN TLTIQVGAND GETIDIDLKQ INSQTLGLDT LNVQQKYKVS DTAATVTGYA DTTIALDNST FKASATGLGG T DQKIDGDL KFDDTTGKYY AKVTVTGGTG KDGYYEVSVD KTNGEVTLAG GATSPLTGGL PATATEDVKN VQVANADLTE AK AALTAAG VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY TADDGTSKTA LNKLGGADGK TEV VSIGGK TYAASKAEGH NFKAQPDLAE AAATTTENPL QKIDAALAQV DTLRSDLGAV QNRFNSAITN LGNTVNNLTS ARSR I UniProtKB: Flagellin |
-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: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |