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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Cryo-EM structure of the LPHT ring | ||||||||||||
![]() | Main map | ||||||||||||
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![]() | Polar flagellum / Polar flagellar motor / LPHT ring / Bushing / MOTOR PROTEIN | ||||||||||||
Function / homology | ![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | ||||||||||||
![]() | Zhang L / Tan JX / Zhou Y / Zhu YQ | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the LPHT ring Authors: Zhang L / Tan JX / Zhou Y / Zhu YQ | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 860 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.3 KB 24.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 20.4 KB | Display | ![]() |
Images | ![]() | 120.5 KB | ||
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() | 842.6 MB 842.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 30 KB | Display | |
Data in CIF | ![]() | 40 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8z5nMC 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 | Main map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.2 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_39776_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_39776_half_map_2.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : The polar flagellar motor-hook complex
Entire | Name: The polar flagellar motor-hook complex |
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Components |
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-Supramolecule #1: The polar flagellar motor-hook complex
Supramolecule | Name: The polar flagellar motor-hook complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Component of sodium-driven polar flagellar motor
Macromolecule | Name: Component of sodium-driven polar flagellar motor / type: protein_or_peptide / ID: 1 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33.528008 KDa |
Sequence | String: MKKWLITSGV VFSLFSTSSF AVMGKRYVAT PQQSQWEMVV NTPLECQLVH PIPSFGDAVF SSRANKKINL DFELKMRRPM GETRNVSLI SMPPPWRPGE HADRITNLKF FKQFDGYVGG QTAWGILSEL EKGRYPTFSY QDWQSRDQRI EVALSSVLFQ N KYNAFSDC ...String: MKKWLITSGV VFSLFSTSSF AVMGKRYVAT PQQSQWEMVV NTPLECQLVH PIPSFGDAVF SSRANKKINL DFELKMRRPM GETRNVSLI SMPPPWRPGE HADRITNLKF FKQFDGYVGG QTAWGILSEL EKGRYPTFSY QDWQSRDQRI EVALSSVLFQ N KYNAFSDC ISNLLKYSFE DIAFTILHYE RQGDQLTKAS KKRLSQIADY IRHNQDIDLV LVATYTDSTD GKSASQSLSE RR AESLRDY FQSLGLPEDR IQVQGYGKRR PIADNGSPIG KDKNRRVVIS LGRTQV UniProtKB: Component of sodium-driven polar flagellar motor |
-Macromolecule #2: Sodium-type flagellar motor component
Macromolecule | Name: Sodium-type flagellar motor component / type: protein_or_peptide / ID: 2 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 24.088613 KDa |
Sequence | String: MKLRTVAASL LLTLVATTAK ANVADVGAPV PIYTEAELIK LIEQNKHLQR VRADNCQLVE DIVARATRIN LPAYEFLYGD MLAWGVCVE QDVELGLYYI ENAAHQGLPA ALEQIGRYYS RGTLVQQDKE RAIPYLREAA SMGNLNARIH LAELLLRDYG S PLDYEDAY ...String: MKLRTVAASL LLTLVATTAK ANVADVGAPV PIYTEAELIK LIEQNKHLQR VRADNCQLVE DIVARATRIN LPAYEFLYGD MLAWGVCVE QDVELGLYYI ENAAHQGLPA ALEQIGRYYS RGTLVQQDKE RAIPYLREAA SMGNLNARIH LAELLLRDYG S PLDYEDAY RWLYNSVTAD KRQHKRITVL RNGLEQRMPQ NVIARAKRRD TFW UniProtKB: Sodium-type flagellar motor component |
-Macromolecule #3: Flagellar L-ring protein
Macromolecule | Name: Flagellar L-ring protein / type: protein_or_peptide / ID: 3 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.929951 KDa |
Sequence | String: MKRICLLALI ATMSGCAMLE PIETDEVTQA TTVVDAVEGD KSKEESSGIV DTLRGRSDPV AGDPAWAPIH PKKKPEHYAA ATGSLFSAE HITDLYDDSK PRGIGDIITV TLDETTSATK SANADLSKTN EAQMDPLQVG GEELQIGGKY NFSYDLNNSN S FAGDSSAK ...String: MKRICLLALI ATMSGCAMLE PIETDEVTQA TTVVDAVEGD KSKEESSGIV DTLRGRSDPV AGDPAWAPIH PKKKPEHYAA ATGSLFSAE HITDLYDDSK PRGIGDIITV TLDETTSATK SANADLSKTN EAQMDPLQVG GEELQIGGKY NFSYDLNNSN S FAGDSSAK QSNSISGYIT VEVIEVLANG NLVIRGEKWM TLNTGDEYIR LSGTIRPDDI SFDNTIASNR VSNARIQYSG TG VQQDMQE PGFLARFFNV AL UniProtKB: UNIPROTKB: A0A9W4BB53 |
-Macromolecule #4: Flagellar assembly lipoprotein FlgP
Macromolecule | Name: Flagellar assembly lipoprotein FlgP / type: protein_or_peptide / ID: 4 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.30376 KDa |
Sequence | String: MKKLLFIVAT LILVGCQPLQ QMRQDEILVA VGYASVSEQT GRTVEEKRVR AMRASKIDAY RELAEQVYGM RVSGRAELQD QRLGIESTT GAVDGVIRGA EVVRSYLVED SYVTELRLDI RKMDKLRDYG EVQQVPEKRQ QTLF UniProtKB: Flagellar assembly lipoprotein FlgP |
-Macromolecule #5: The N-terminus of Flagellar L-ring protein
Macromolecule | Name: The N-terminus of Flagellar L-ring protein / type: protein_or_peptide / ID: 5 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.45063 KDa |
Sequence | String: CAMLEPIETD EVT |
-Macromolecule #6: Flagellar P-ring protein
Macromolecule | Name: Flagellar P-ring protein / type: protein_or_peptide / ID: 6 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 37.892234 KDa |
Sequence | String: MKKLLLILMS VALFSTAAQA ARIKDVAQVA GVRSNQLVGY GLVSGLPGTG EANPFTEQSF AAMLQNFGIQ MPPGTKPKIK NVAAVMVTA ELPPFSKPGQ QVDVTVSSIG SAKSLRGGTL LQTFLKGLDG QVYAVAQGNL VVSGFSAEGA DGSKIVGNNP T VGLISSGA ...String: MKKLLLILMS VALFSTAAQA ARIKDVAQVA GVRSNQLVGY GLVSGLPGTG EANPFTEQSF AAMLQNFGIQ MPPGTKPKIK NVAAVMVTA ELPPFSKPGQ QVDVTVSSIG SAKSLRGGTL LQTFLKGLDG QVYAVAQGNL VVSGFSAEGA DGSKIVGNNP T VGLISSGA TVEREIPNPF GRGDYITFNL LESDFTTAQR MADAVNNFLG PQMASAVDAT SVRVRAPRDV SQRVAFLSAI EN LEFDPAD GAAKIIVNSR TGTIVVGKHV RLKPAAVTHG GMTVAIKENL NVSQPNGFSG GQTVVVPDSD IEVSEEQGKM FKF EPGLTL DDLVRAVNQV GAAPSDLMAI LQALKQAGAI EGQLIII UniProtKB: UNIPROTKB: A0A9W4BSQ4 |
-Macromolecule #7: Flagella basal-body protein
Macromolecule | Name: Flagella basal-body protein / type: protein_or_peptide / ID: 7 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 42.417168 KDa |
Sequence | String: MKKILNSLFS ITLVMLVPFK VMASWYEVTG VATIVSSEET ARLHALEDAL FKAVNFSGAD IGSISNLMPL LEESRNEYQF TNHEVRYIL VESERKRRGK VEVKIRVDIY PSATGCHTDQ YKKTILVGNI EVASPQQAVM GQIYQVGDDF SRVVNRQLDQ T SRSFVSVG ...String: MKKILNSLFS ITLVMLVPFK VMASWYEVTG VATIVSSEET ARLHALEDAL FKAVNFSGAD IGSISNLMPL LEESRNEYQF TNHEVRYIL VESERKRRGK VEVKIRVDIY PSATGCHTDQ YKKTILVGNI EVASPQQAVM GQIYQVGDDF SRVVNRQLDQ T SRSFVSVG TTDYSISSNY PARTQMIAQD NGAQYIIGGV ITDLTATVES QLLQDDIINR QFALEMKVFD GKTGHEVFNK AY REVARWP FAKTSQVDTR SARFWASTYG EMMLRVSRNI MLDLESELSC KITLPEVVAV FGNTVTMDLG RMHGVKEGDK LQL WHTASF IDQNGLPRNK VSQSEITLTV SRIYEHEAEL TIDQPNLASS VQIGDVMNKI L UniProtKB: Flagella basal-body protein |
-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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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV |
Image recording | Film or detector model: FEI FALCON IV (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: 1.8 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
Output model | ![]() PDB-8z5n: |