[English] 日本語
Yorodumi
- EMDB-72847: LPHT-ring in Vibrio cholerae at disassembled, closed state -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-72847
TitleLPHT-ring in Vibrio cholerae at disassembled, closed state
Map data
Sample
  • Cell: Vibrio cholerae DflhG
    • Protein or peptide: Flagellar L-ring protein
    • Protein or peptide: Flagellar P-ring protein
    • Protein or peptide: Flagellar protein FlgT
    • Protein or peptide: Sodium-type flagellar protein MotY
    • Protein or peptide: Sodium-type flagellar protein MotX
    • Protein or peptide: Lipoprotein
KeywordsIn situ cryo-EM / sheathed flagellar motor / Vibrio cholerae / T-ring / MotX / C26 assembled state / MOTOR PROTEIN
Function / homology
Function and homology information


bacterial-type flagellum basal body, distal rod, L ring / bacterial-type flagellum basal body, distal rod, P ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / cell outer membrane / outer membrane-bounded periplasmic space / structural molecule activity
Similarity search - Function
Flagellar assembly protein T, N-terminal / Flagellar assembly protein T, middle domain / Flagellar assembly protein T, C-terminal / FlgT, C-terminal domain superfamily / Flagellar assembly protein T, C-terminal domain / Flagellar assembly protein T, middle domain / Flagellar assembly protein T, N-terminal domain / FlgT, N-terminal domain superfamily / MotY N-terminal domain / MotY N-terminal domain ...Flagellar assembly protein T, N-terminal / Flagellar assembly protein T, middle domain / Flagellar assembly protein T, C-terminal / FlgT, C-terminal domain superfamily / Flagellar assembly protein T, C-terminal domain / Flagellar assembly protein T, middle domain / Flagellar assembly protein T, N-terminal domain / FlgT, N-terminal domain superfamily / MotY N-terminal domain / MotY N-terminal domain / Flagellar protein FlgP / Flagellar L-ring protein / Flagellar L-ring protein / Flagellar P-ring protein / Flagellar P-ring protein / : / Sel1 repeat / Sel1-like repeat / Sel1-like repeats. / : / OmpA-like domain profile. / OmpA family / OmpA-like domain / OmpA-like domain superfamily / Prokaryotic membrane lipoprotein lipid attachment site profile. / Tetratricopeptide-like helical domain superfamily
Similarity search - Domain/homology
Sodium-type flagellar protein MotX / Flagellar protein FlgT / Lipoprotein / Flagellar L-ring protein / Flagellar P-ring protein / Sodium-type flagellar protein MotY
Similarity search - Component
Biological speciesVibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.57 Å
AuthorsGuo W / Yue J
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI087946 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI132818 United States
CitationJournal: To Be Published
Title: In-situ cryo-EM structures reveal mechanisms of sheathed flagellar assembly, rotation, and disassembly in Vibrio cholerae
Authors: Wangbiao G / Jian Y / Jin HP / Fitnat Y / Jun L
History
DepositionSep 24, 2025-
Header (metadata) releaseJun 10, 2026-
Map releaseJun 10, 2026-
UpdateJun 10, 2026-
Current statusJun 10, 2026Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_72847.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 448 pix.
= 478.464 Å
1.07 Å/pix.
x 448 pix.
= 478.464 Å
1.07 Å/pix.
x 448 pix.
= 478.464 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.068 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.3868437 - 0.8472436
Average (Standard dev.)0.012706139 (±0.065536745)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 478.464 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_72847_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Additional map: #1

Fileemd_72847_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_72847_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_72847_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Vibrio cholerae DflhG

EntireName: Vibrio cholerae DflhG
Components
  • Cell: Vibrio cholerae DflhG
    • Protein or peptide: Flagellar L-ring protein
    • Protein or peptide: Flagellar P-ring protein
    • Protein or peptide: Flagellar protein FlgT
    • Protein or peptide: Sodium-type flagellar protein MotY
    • Protein or peptide: Sodium-type flagellar protein MotX
    • Protein or peptide: Lipoprotein

-
Supramolecule #1: Vibrio cholerae DflhG

SupramoleculeName: Vibrio cholerae DflhG / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)

-
Macromolecule #1: Flagellar L-ring protein

MacromoleculeName: Flagellar L-ring protein / type: protein_or_peptide / ID: 1 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 27.54148 KDa
SequenceString: MKRLLASSLL ILLSGCSLMQ PPIESAETIQ GTTTVDAVEG DKSESNSGLT DALRNRTDPV AGDPAWAPIH PKGKPEHYAA ETGSLFNLA SSSSMYDDSK PRGVGDIITV TLNESTKAAK SADADLNKKN DASMDPLAVG GKDLTIGDYN FSYALKNDNK F SGSAAANQ ...String:
MKRLLASSLL ILLSGCSLMQ PPIESAETIQ GTTTVDAVEG DKSESNSGLT DALRNRTDPV AGDPAWAPIH PKGKPEHYAA ETGSLFNLA SSSSMYDDSK PRGVGDIITV TLNESTKAAK SADADLNKKN DASMDPLAVG GKDLTIGDYN FSYALKNDNK F SGSAAANQ SNSMSGSITV EVIEVLANGN LVIRGEKWLT LNTGDEYIRL SGTIRPDDID FDNTIASNRI SNARIQYSGT GT NQDMQEP GFLARFFNVS L

UniProtKB: Flagellar L-ring protein

-
Macromolecule #2: Flagellar P-ring protein

MacromoleculeName: Flagellar P-ring protein / type: protein_or_peptide / ID: 2 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 37.694059 KDa
SequenceString: MRKFTILLML LLASSAQAAR IKDVAQVAGV RNNQLVGYGL VTGLPGTGES TPFTDQSFNA MLQSFGIQLP PGTKPKTKNV AAVIVTADL PAFSKQGQTI DITVSSIGSA KSLRGGTLMQ TFLKGLDGQV YAVAQGNLVV SGFSATGADG SKIVGNNPTV G MISSGAIV ...String:
MRKFTILLML LLASSAQAAR IKDVAQVAGV RNNQLVGYGL VTGLPGTGES TPFTDQSFNA MLQSFGIQLP PGTKPKTKNV AAVIVTADL PAFSKQGQTI DITVSSIGSA KSLRGGTLMQ TFLKGLDGQV YAVAQGNLVV SGFSATGADG SKIVGNNPTV G MISSGAIV EREVPNPFGR GDYITFNLFE SDFTTAQRLA DAVNQFLGPQ MASAVDAASI KVRAPRDLSQ RVAFLSAIEN LE FNPADSA AKIIVNSRTG TIVVGQNVRL KPAAVTHGGM TVAIKENLNV SQPNALGGGQ TVVVPNTEIE VTEKQGKMFK LEP GVTLDD LVRAVNEVGA APSDLMAILQ ALKQAGAIEG QLIII

UniProtKB: Flagellar P-ring protein

-
Macromolecule #3: Flagellar protein FlgT

MacromoleculeName: Flagellar protein FlgT / type: protein_or_peptide / ID: 3 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 42.647734 KDa
SequenceString: MKKNILSIIS ALWMMLQLPS AHAAWYEVTG SAAIVSSEEV ARLHALEDAL YKAVNFAGAD IGSISNLMPL LESDRREYLF ANHEVRYIL IEERKAINNV MYVRTRIDIY PSATACHVEQ YKKTMLIGNI DLASPQQAVM GQIYQVGDDF AQVINRRLEQ E SRSFVSVG ...String:
MKKNILSIIS ALWMMLQLPS AHAAWYEVTG SAAIVSSEEV ARLHALEDAL YKAVNFAGAD IGSISNLMPL LESDRREYLF ANHEVRYIL IEERKAINNV MYVRTRIDIY PSATACHVEQ YKKTMLIGNI DLASPQQAVM GQIYQVGDDF AQVINRRLEQ E SRSFVSVG TTQYDIDPKA PERIKMIAQD AGAQYIMGGM ITDLTATIEQ KTLQDDIINR QFAMEISVFD GKTGNEVMTR TY REVARWP FPKTSQIDTR SARFWASTYG EMMLRVSRNI MLDLESEISC KITLPQIVAK FGTTATMDLG RIHGVKQGDK LSL WHTGAF IDQQGLPRNK VTQSEITLTV SRVYEHEAEL TVDQPELAYS IQIGDVMHKQ M

UniProtKB: Flagellar protein FlgT

-
Macromolecule #4: Sodium-type flagellar protein MotY

MacromoleculeName: Sodium-type flagellar protein MotY / type: protein_or_peptide / ID: 4 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 33.587746 KDa
SequenceString: MNKWVITSLF AISTLSASVA SALEVRYMAT PQQSTWQMAT NTPLECRLVH PIPNYGDAEF SSRAGKKINL DFELKMRRPM GDTRNVSLV SMPPVWRPGE GADRITNLQF FKQFDGYIGG QTAWSLLSEL EKGRYPTFSY QDWQSRDQRI EVALSSVLFQ Q PYNEFSDC ...String:
MNKWVITSLF AISTLSASVA SALEVRYMAT PQQSTWQMAT NTPLECRLVH PIPNYGDAEF SSRAGKKINL DFELKMRRPM GDTRNVSLV SMPPVWRPGE GADRITNLQF FKQFDGYIGG QTAWSLLSEL EKGRYPTFSY QDWQSRDQRI EVALSSVLFQ Q PYNEFSDC ISKLLPYSFE DISFTILHYD QGTSVELNKA SQKRLAQIAE YVRYNQDIDL VLVSTYTDST DTNNNSQNLS EQ RAEVLRE YFKSIGLPED RIQVQGYGKR RPIADNASPI GKDKNRRVVI SLGRTQV

UniProtKB: Sodium-type flagellar protein MotY

-
Macromolecule #5: Sodium-type flagellar protein MotX

MacromoleculeName: Sodium-type flagellar protein MotX / type: protein_or_peptide / ID: 5 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 24.278615 KDa
SequenceString: MKLRTVAASL LLAWHSSYNP AYAADLGEPV PIYSEAELIK LIEENKHLER VKADNCQIVE DIVARATRIS LPSYEFLYGD MLAWGVCVD QDVELGLYYM ENAAHQGLPA ALEQLGRYYS RGTLVQQDKE RAIPYLREAA AMGNLNARIQ LAELLLRDYG S PLDYEDAY ...String:
MKLRTVAASL LLAWHSSYNP AYAADLGEPV PIYSEAELIK LIEENKHLER VKADNCQIVE DIVARATRIS LPSYEFLYGD MLAWGVCVD QDVELGLYYM ENAAHQGLPA ALEQLGRYYS RGTLVQQDKE RAIPYLREAA AMGNLNARIQ LAELLLRDYG S PLDYEDAY RWLYNSVTAD QRTHNRIALL RQGLERRMPE NIIARAKRRE TFW

UniProtKB: Sodium-type flagellar protein MotX

-
Macromolecule #6: Lipoprotein

MacromoleculeName: Lipoprotein / type: protein_or_peptide / ID: 6 / Number of copies: 52 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
Molecular weightTheoretical: 16.459971 KDa
SequenceString:
MMKSSLLLLV AALMMTGCQP LQSMRPDDWL TAVGYANISE QRGRDEAEKQ VRAMRASKID AYRELAEQVY GMRISGRAEL QDQRLGTEL TAGAVDGVIR GAEVVRSYKV GDSYVTELRL DIRKMDKMRD YGEVQQVPEK RQMTLF

UniProtKB: Lipoprotein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statecell

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE-PROPANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 70.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.6 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C13 (13 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.57 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 25553
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more