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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Campylobacter hook-filament junction-cap complex | |||||||||
![]() | Campylobacter cap-junction complex | |||||||||
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![]() | Campylobacter jejuni / flagellar cap / hook-filament junction / FliD / FlgK / FlgL / flagella / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum filament cap / bacterial-type flagellum hook / bacterial-type flagellum / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / cell adhesion / structural molecule activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.5 Å | |||||||||
![]() | Qin K / Gonzalez-Rodriguez N / Shmakova E / Beeby M / Bergeron JRC | |||||||||
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 / Gonzalez-Rodriguez N / Harrowell J / Shmakova E / Beeby M / Erhardt M / Bergeron JRC | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 96.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.1 KB 18.1 KB | Display Display | ![]() |
Images | ![]() | 102.5 KB | ||
Filedesc metadata | ![]() | 6.6 KB | ||
Others | ![]() ![]() | 81.5 MB 81.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9gsxMC ![]() 9gnzC ![]() 9go6C 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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Annotation | Campylobacter cap-junction complex | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.2 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map 1
File | emd_51557_half_map_1.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 2
File | emd_51557_half_map_2.map | ||||||||||||
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Annotation | Half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Hook-filament junction-cap complex in Campylobacter jejuni
Entire | Name: Hook-filament junction-cap complex in Campylobacter jejuni |
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Components |
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-Supramolecule #1: Hook-filament junction-cap complex in Campylobacter jejuni
Supramolecule | Name: Hook-filament junction-cap complex in Campylobacter jejuni type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 11 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 82.047 KDa |
Sequence | String: MRITNKLNFT NSVNNSMGGQ SALYQISQQL ASGLKIQNSY EDASTYIDNT RLEYEIKTLE QVKESTSRAQ EMTQNSMKAL QDMVKLLED FKVKVTQAAS DSNSQTSREA IAKELERIKE SIVQLANTSV NGQYLFAGSQ VANKPFDSNG NYYGDKNNIN V VTGAGTES ...String: MRITNKLNFT NSVNNSMGGQ SALYQISQQL ASGLKIQNSY EDASTYIDNT RLEYEIKTLE QVKESTSRAQ EMTQNSMKAL QDMVKLLED FKVKVTQAAS DSNSQTSREA IAKELERIKE SIVQLANTSV NGQYLFAGSQ VANKPFDSNG NYYGDKNNIN V VTGAGTES PYNIPGWDLF FKADGDYKKQ ISTNVSFTDN RWDLNKDPDK TKYLTGDSKW QQLIGQGYVK DNSLDADKDF EY DDSKLDF PPTTLYVQGT KPDGTSFKSA VLVKPEDTLE DVMENIGALY GNTPNNKVVE VSMNDSGQIQ ITDLKQGNNK LDF HAVAFT PQADTKDELK NIIEAANQEG ISMNEVTNRV MQASTAAPSN GDITKLNNPV TVTINNQQFT IDLKQTDFIK SKMT DTDGN AANGADYDNV YFEKNGNTVY GNVSQVIKGS NAYATDSTKL SEVMAGDSLN GTTLNLKVNS KGGNSYDVTI NLQTS TVSY PDPNNPGQTI SFPIMHTNPA TGNSGVVTGS NDITYGQIND IIGMFAADKI PTTTIQANNG QINNADYTQI QQLMKD SQA TVDVSMDYKG RISVTDKLSS GTNIEISLSD SQSGQFPAPP FTTTSTVQNG PNFSFSANNS LTIDEPNVDI IKDLDSM ID AVLKGNMRAD SESENPRNTG MQGALERLDH LADHVSKLNT TMGAYHNTIE GVNTRTSFLS VNVQSIKSNV IDVDYGEA M MNLMQVQLAY QASLKASTTI SQLSLLNYM UniProtKB: Flagellin |
-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: 67.121469 KDa |
Sequence | String: MGIFGTLYTG VTGLKASEVQ IATTGNNISN ANATFYTRQR VVQTTNGYIT TGGVQVGTGT AVESIVRLHD EYSYYKLKGA SNQLEYTKY MASTLQEIAQ RFPDLQNTGI LQDLENYNKA WNDFASNPNE NATKIALVKA SQTLTESVNN TFATLDKIQK K VNDDIKNT ...String: MGIFGTLYTG VTGLKASEVQ IATTGNNISN ANATFYTRQR VVQTTNGYIT TGGVQVGTGT AVESIVRLHD EYSYYKLKGA SNQLEYTKY MASTLQEIAQ RFPDLQNTGI LQDLENYNKA WNDFASNPNE NATKIALVKA SQTLTESVNN TFATLDKIQK K VNDDIKNT VDEINKIGEE IATINKQIYG QEALPTEHAN ELRDRRDELE LTLSKLVSAV ASKNEINQDN RLDTTITDPG HQ YNLSIEG FSIVDGINFH PLKLDYDDKN KSYSIYYETP DEKVRDLTAK ISGGQLGAQL DLRGRNYSKS EGKYEDGIIQ GYM DSLDTF AKTMINETNN LYASSAKSSV TSDYLSGLKG DIPLVNYDRT IQPGSFDIVI YDDKGDKKLT KTITIDVNTT MNDI MRQIN ANTDDNDNKN SNDDVDDHIN ASFSYDAKTG DGLFQINAKS GFKVAIEDKG TNFAGAFSIG GFFSGTDASD MKVKD SILN DPSTVRASSN GVDSGNDMAN KIIQLQYDKV NFYNEDGTID NLTMEEYYRK LTGKIASDGE NNNVVNSSNE TLYNSV YSE YQSKSGVNTN EELAALIQYQ SSYGAAAKIV STVDQMLDTL LGLKS UniProtKB: Flagellar hook-associated protein 1 |
-Macromolecule #3: Flagellar hook-associated protein 2
Macromolecule | Name: Flagellar hook-associated protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 69.843852 KDa |
Sequence | String: MAFGSLSSLG FGSGVLTQDT IDKLKEAEQK ARIDPYTKKI EENTTKQKDL TEIKTKLLSF QTAVSSLADA TVFAKRKVVG SISDNPPAS LTVNSGVALQ SMNINVTQLA QKDVYQSKGL ANDGGFVNAQ LNGTADLTFF SNGKEYTVTV DKNTTYRDLA D KINEASGG ...String: MAFGSLSSLG FGSGVLTQDT IDKLKEAEQK ARIDPYTKKI EENTTKQKDL TEIKTKLLSF QTAVSSLADA TVFAKRKVVG SISDNPPAS LTVNSGVALQ SMNINVTQLA QKDVYQSKGL ANDGGFVNAQ LNGTADLTFF SNGKEYTVTV DKNTTYRDLA D KINEASGG EIVAKIVNTG EKGTPYRLTL TSKETGEDSA ISFYAGKKDS NGKYQKDINA EKIFDDLGWG LDVSASIDPD KD KKGYGIK DASLHIQTAQ NAEFTLDGIK MFRSSNTVTD LGVGMTLTLN KTGEINFDVQ QDFEGVTKAM QDLVDAYNDL VTN LNAATD YNSETGTKGT LQGISEVNSI RSSILADLFD SQVVDGTTED ANGNKVNTKV MLSMQDFGLS LNDAGTLSFD SSKF EQKVK EDPDSTESFF SNITKYEDIN HTGEVIKTGS LSKYLNSNGG NTNGLEFKPG DFTIVFNNQT YDLSKNSDGT NFKLT GKTE EELLQNLANH INSKGIEGLK VKVESYNQNN VTGFRLNFSG DGSSDFSIKG DANILKELGL SDVNITSKPI EGKGIF SKL KATLQEMTGK DGSITKYDES LTNDIKSLNT SKDSTQAMID TRYDTMANQW LQYESILNKL NQQLNTVTNM INAANNS NN UniProtKB: Flagellar hook-associated protein 2 |
-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: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
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 | Resolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 15077 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |