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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Salmonella hook-filament junction complex | |||||||||
![]() | Salmonella hook-filament junction at its native context | |||||||||
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![]() | Bacterial flagellum / Hook-filament junction / FlgK / FlgL / Salmonella enterica / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum hook / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / structural molecule activity / extracellular region / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Qin K / Einenkel R / Erhardt E / Bergeron JR | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure of the complete extracellular bacterial flagellum reveals mechanism for flagellin incorporation Authors: Qin K / Einenkel R / Al-Otaibi NS / Schmidt J / Mann D / Drobnic T / Cohen EJ / Rodriguez NG / Harrowell J / Shmakova E / Beeby E / Erhardt E / Bergeron JR | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 449.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.6 KB 19.6 KB | Display Display | ![]() |
Images | ![]() | 158.5 KB | ||
Filedesc metadata | ![]() | 6.6 KB | ||
Others | ![]() ![]() | 442.1 MB 442.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9go6MC ![]() 9gnzC ![]() 9gsxC 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
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Salmonella hook-filament junction at its native context | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.078 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map A
File | emd_51493_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_51493_half_map_2.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Shorten flagella of Salmonella enterica
Entire | Name: Shorten flagella of Salmonella enterica |
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Components |
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-Supramolecule #1: Shorten flagella of Salmonella enterica
Supramolecule | Name: Shorten flagella of Salmonella enterica / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.13 MDa |
-Macromolecule #1: Flagellar hook protein FlgE
Macromolecule | Name: Flagellar hook protein FlgE / type: protein_or_peptide / ID: 1 / Number of copies: 13 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 42.233152 KDa |
Sequence | String: MSFSQAVSGL NAAATNLDVI GNNIANSATY GFKSGTASFA DMFAGSKVGL GVKVAGITQD FTDGTTTNTG RGLDVAISQN GFFRLVDSN GSVFYSRNGQ FKLDENRNLV NMQGMQLTGY PATGTPPTIQ QGANPAPITI PNTLMAAKST TTASMQINLN S TDPVPSKT ...String: MSFSQAVSGL NAAATNLDVI GNNIANSATY GFKSGTASFA DMFAGSKVGL GVKVAGITQD FTDGTTTNTG RGLDVAISQN GFFRLVDSN GSVFYSRNGQ FKLDENRNLV NMQGMQLTGY PATGTPPTIQ QGANPAPITI PNTLMAAKST TTASMQINLN S TDPVPSKT PFSVSDADSY NKKGTVTVYD SQGNAHDMNV YFVKTKDNEW AVYTHDSSDP AATAPTTAST TLKFNENGIL ES GGTVNIT TGTINGATAA TFSLSFLNSM QQNTGANNIV ATNQNGYKPG DLVSYQINND GTVVGNYSNE QEQVLGQIVL ANF ANNEGL ASQGDNVWAA TQASGVALLG TAGSGNFGKL TNGALEASNV DLSKELVNMI VAQRNYQSNA QTIKTQDQIL NTLV NLR UniProtKB: Flagellar hook protein FlgE |
-Macromolecule #2: Flagellar hook-associated protein 1
Macromolecule | Name: Flagellar hook-associated protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 11 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 59.153781 KDa |
Sequence | String: MSSLINHAMS GLNAAQAALN TVSNNINNYN VAGYTRQTTI LAQANSTLGA GGWIGNGVYV SGVQREYDAF ITNQLRGAQN QSSGLTTRY EQMSKIDNLL ADKSSSLSGS LQSFFTSLQT LVSNAEDPAA RQALIGKAEG LVNQFKTTDQ YLRDQDKQVN I AIGSSVAQ ...String: MSSLINHAMS GLNAAQAALN TVSNNINNYN VAGYTRQTTI LAQANSTLGA GGWIGNGVYV SGVQREYDAF ITNQLRGAQN QSSGLTTRY EQMSKIDNLL ADKSSSLSGS LQSFFTSLQT LVSNAEDPAA RQALIGKAEG LVNQFKTTDQ YLRDQDKQVN I AIGSSVAQ INNYAKQIAN LNDQISRMTG VGAGASPNDL LDQRDQLVSE LNKIVGVEVS VQDGGTYNLT MANGYTLVQG ST ARQLAAV PSSADPTRTT VAYVDEAAGN IEIPEKLLNT GSLGGLLTFR SQDLDQTRNT LGQLALAFAD AFNAQHTKGY DAD GNKGKD FFSIGSPVVY SNSNNADKTV SLTAKVVDST KVQATDYKIV FDGTDWQVTR TADNTTFTAT KDADGKLEID GLKV TVGTG AQKNDSFLLK PVSNAIVDMN VKVTNEAEIA MASESKLDPD VDTGDSDNRN GQALLDLQNS NVVGGNKTFN DAYAT LVSD VGNKTSTLKT SSTTQANVVK QLYKQQQSVS GVNLDEEYGN LQRYQQYYLA NAQVLQTANA LFDALLNIR UniProtKB: Flagellar hook-associated protein 1 |
-Macromolecule #3: Flagellar hook-associated protein
Macromolecule | Name: Flagellar hook-associated protein / type: protein_or_peptide / ID: 3 / Number of copies: 11 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 34.201965 KDa |
Sequence | String: MRISTQMMYE QNMSGITNSQ AEWMKLGEQM STGKRVTNPS DDPIAASQAV VLSQAQAQNS QYALARTFAT QKVSLEESVL SQVTTAIQT AQEKIVYAGN GTLSDDDRAS LATDLQGIRD QLMNLANSTD GNGRYIFAGY KTEAAPFDQA TGGYHGGEKS V TQQVDSAR ...String: MRISTQMMYE QNMSGITNSQ AEWMKLGEQM STGKRVTNPS DDPIAASQAV VLSQAQAQNS QYALARTFAT QKVSLEESVL SQVTTAIQT AQEKIVYAGN GTLSDDDRAS LATDLQGIRD QLMNLANSTD GNGRYIFAGY KTEAAPFDQA TGGYHGGEKS V TQQVDSAR TMVIGHTGAQ IFNSITSNAV PEPDGSDSEK NLFVMLDTAI AALKTPVEGN NVEKEKAAAA IDKTNRGLKN SL NNVLTVR AELGTQLSEL STLDSLGSDR ALGQKLQMSN LVDVDWNSVI SSYVMQQAAL QASYKTFTDM QGMSLFQLNR UniProtKB: Flagellar hook-associated protein |
-Macromolecule #4: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 4 / Number of copies: 15 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 51.654344 KDa |
Sequence | String: MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNL QRVRELAVQS ANSTNSQSDL DSIQAEITQR LNEIDRVSGQ TQFNGVKVLA QDNTLTIQVG ANDGETIDID L KQINSQTL ...String: MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNL QRVRELAVQS ANSTNSQSDL DSIQAEITQR LNEIDRVSGQ TQFNGVKVLA QDNTLTIQVG ANDGETIDID L KQINSQTL GLDTLNVQQK YKVSDTAATV TGYADTTIAL DNSTFKASAT GLGGTDQKID GDLKFDDTTG KYYAKVTVTG GT GKDGYYE VSVDKTNGEV TLAGGATSPL TGGLPATATE DVKNVQVANA DLTEAKAALT AAGVTGTASV VKMSYTDNNG KTI DGGLAV KVGDDYYSAT QNKDGSISIN TTKYTADDGT SKTALNKLGG ADGKTEVVSI GGKTYAASKA EGHNFKAQPD LAEA AATTT ENPLQKIDAA LAQVDTLRSD LGAVQNRFNS AITNLGNTVN NLTSARSRIE DSDYATEVSN MSRAQILQQA GTSVL AQAN QVPQNVLSLL R UniProtKB: Flagellin |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 88 % / Chamber temperature: 277 K / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 0.9 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Number classes used: 1 / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 65561 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |