[English] 日本語
Yorodumi
- EMDB-39742: Cryo-EM structure of Escherichia coli OppBCDF in the resting state -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-39742
TitleCryo-EM structure of Escherichia coli OppBCDF in the resting state
Map data
Sample
  • Complex: OppBCDF heterotetramer
    • Protein or peptide: Oligopeptide transport system permease protein OppB
    • Protein or peptide: Oligopeptide transport system permease protein OppC
    • Protein or peptide: Oligopeptide transport ATP-binding protein OppD
    • Protein or peptide: Oligopeptide transport ATP-binding protein OppF
  • Ligand: IRON/SULFUR CLUSTER
KeywordsABC importer / oligopeptide transporter / TRANSPORT PROTEIN
Function / homology
Function and homology information


peptidoglycan-associated peptide transport / oligopeptide import across plasma membrane / peptidoglycan peptide transmembrane transporter activity / ABC-type oligopeptide transporter / tripeptide import across plasma membrane / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / protein transport / ATP hydrolysis activity / ATP binding / membrane / plasma membrane
Similarity search - Function
: / Oligopeptide transport permease C-like, N-terminal domain / N-terminal TM domain of oligopeptide transport permease C / ABC transporter type 1, GsiC-like, N-terminal domain / : / : / Binding-prot-dependent transport system membrane comp, N-term / Oligopeptide/dipeptide ABC transporter, C-terminal / Oligopeptide/dipeptide transporter, C-terminal region / ABC transporter type 1, transmembrane domain MetI-like ...: / Oligopeptide transport permease C-like, N-terminal domain / N-terminal TM domain of oligopeptide transport permease C / ABC transporter type 1, GsiC-like, N-terminal domain / : / : / Binding-prot-dependent transport system membrane comp, N-term / Oligopeptide/dipeptide ABC transporter, C-terminal / Oligopeptide/dipeptide transporter, C-terminal region / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Oligopeptide transport system permease protein OppB / Oligopeptide transport system permease protein OppC / Oligopeptide transport ATP-binding protein OppD / Oligopeptide transport ATP-binding protein OppF
Similarity search - Component
Biological speciesEscherichia coli (strain K12) (bacteria) / Escherichia coli K-12 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.17 Å
AuthorsLi P / Huang Y
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: To Be Published
Title: Cryo-EM structure of Escherichia coli OppBCDF in the resting state
Authors: Li P / Huang Y
History
DepositionApr 12, 2024-
Header (metadata) releaseApr 16, 2025-
Map releaseApr 16, 2025-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_39742.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.52 Å/pix.
x 512 pix.
= 266.24 Å
0.52 Å/pix.
x 512 pix.
= 266.24 Å
0.52 Å/pix.
x 512 pix.
= 266.24 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.52 Å
Density
Contour LevelBy AUTHOR: 0.07
Minimum - Maximum-0.0016853233 - 2.8093698
Average (Standard dev.)0.0012334933 (±0.026506731)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 266.24 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_39742_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_39742_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : OppBCDF heterotetramer

EntireName: OppBCDF heterotetramer
Components
  • Complex: OppBCDF heterotetramer
    • Protein or peptide: Oligopeptide transport system permease protein OppB
    • Protein or peptide: Oligopeptide transport system permease protein OppC
    • Protein or peptide: Oligopeptide transport ATP-binding protein OppD
    • Protein or peptide: Oligopeptide transport ATP-binding protein OppF
  • Ligand: IRON/SULFUR CLUSTER

-
Supramolecule #1: OppBCDF heterotetramer

SupramoleculeName: OppBCDF heterotetramer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Escherichia coli (strain K12) (bacteria)
Molecular weightTheoretical: 140 KDa

-
Macromolecule #1: Oligopeptide transport system permease protein OppB

MacromoleculeName: Oligopeptide transport system permease protein OppB / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 33.47307 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLKFILRRCL EAIPTLFILI TISFFMMRLA PGSPFTGERT LPPEVMANIE AKYHLNDPIM TQYFSYLKQL AHGDFGPSFK YKDYSVNDL VASSFPVSAK LGAAAFFLAV ILGVSAGVIA ALKQNTKWDY TVMGLAMTGV VIPSFVVAPL LVMIFAIILH W LPGGGWNG ...String:
MLKFILRRCL EAIPTLFILI TISFFMMRLA PGSPFTGERT LPPEVMANIE AKYHLNDPIM TQYFSYLKQL AHGDFGPSFK YKDYSVNDL VASSFPVSAK LGAAAFFLAV ILGVSAGVIA ALKQNTKWDY TVMGLAMTGV VIPSFVVAPL LVMIFAIILH W LPGGGWNG GALKFMILPM VALSLAYIAS IARITRGSMI EVLHSNFIRT ARAKGLPMRR IILRHALKPA LLPVLSYMGP AF VGIITGS MVIETIYGLP GIGQLFVNGA LNRDYSLVLS LTILVGALTI LFNAIVDVLY AVIDPKIRY

UniProtKB: Oligopeptide transport system permease protein OppB

-
Macromolecule #2: Oligopeptide transport system permease protein OppC

MacromoleculeName: Oligopeptide transport system permease protein OppC / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 33.046781 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MMLSKKNSET LENFSEKLEV EGRSLWQDAR RRFMHNRAAV ASLIVLVLIA LFVILAPMLS QFAYDDTDWA MMSSAPDMES GHYFGTDSS GRDLLVRVAI GGRISLMVGV AAALVAVVVG TLYGSLSGYL GGKVDSVMMR LLEILNSFPF MFFVILLVTF F GQNILLIF ...String:
MMLSKKNSET LENFSEKLEV EGRSLWQDAR RRFMHNRAAV ASLIVLVLIA LFVILAPMLS QFAYDDTDWA MMSSAPDMES GHYFGTDSS GRDLLVRVAI GGRISLMVGV AAALVAVVVG TLYGSLSGYL GGKVDSVMMR LLEILNSFPF MFFVILLVTF F GQNILLIF VAIGMVSWLD MARIVRGQTL SLKRKEFIEA AQVGGVSTSG IVIRHIVPNV LGVVVVYASL LVPSMILFES FL SFLGLGT QEPLSSWGAL LSDGANSMEV SPWLLLFPAG FLVVTLFCFN FIGDGLRDAL DPKDR

UniProtKB: Oligopeptide transport system permease protein OppC

-
Macromolecule #3: Oligopeptide transport ATP-binding protein OppD

MacromoleculeName: Oligopeptide transport ATP-binding protein OppD / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: ABC-type oligopeptide transporter
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 37.114207 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSVIETATVP LAQQQADALL NVKDLRVTFS TPDGDVTAVN DLNFSLRAGE TLGIVGESGS GKSQTAFALM GLLAANGRIG GSATFNGRE ILNLPEHELN KLRAEQISMI FQDPMTSLNP YMRVGEQLME VLMLHKNMSK AEAFEESVRM LDAVKMPEAR K RMKMYPHE ...String:
MSVIETATVP LAQQQADALL NVKDLRVTFS TPDGDVTAVN DLNFSLRAGE TLGIVGESGS GKSQTAFALM GLLAANGRIG GSATFNGRE ILNLPEHELN KLRAEQISMI FQDPMTSLNP YMRVGEQLME VLMLHKNMSK AEAFEESVRM LDAVKMPEAR K RMKMYPHE FSGGMRQRVM IAMALLCRPK LLIADEPTTA LDVTVQAQIM TLLNELKREF NTAIIMITHD LVVVAGICDK VL VMYAGRT MEYGNARDVF YQPVHPYSIG LLNAVPRLDA EGETMLTIPG NPPNLLRLPK GCPFQPRCPH AMEICSSAPP LEE FTPGRL RACFKPVEEL

UniProtKB: Oligopeptide transport ATP-binding protein OppD

-
Macromolecule #4: Oligopeptide transport ATP-binding protein OppF

MacromoleculeName: Oligopeptide transport ATP-binding protein OppF / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: ABC-type oligopeptide transporter
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 37.133352 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MNAVTEGRKV LLEIADLKVH FEIKDGKQWF WQPPKTLKAV DGVTLRLYEG ETLGVVGESG CGKSTFARAI IGLVKATDGH VAWLGKELL GMKPDEWRAV RSDIQMIFQD PLASLNPRMT IGEIIAEPLR TYHPKMSRQE VRERVKAMML KVGLLPNLIN R YPHEFSGG ...String:
MNAVTEGRKV LLEIADLKVH FEIKDGKQWF WQPPKTLKAV DGVTLRLYEG ETLGVVGESG CGKSTFARAI IGLVKATDGH VAWLGKELL GMKPDEWRAV RSDIQMIFQD PLASLNPRMT IGEIIAEPLR TYHPKMSRQE VRERVKAMML KVGLLPNLIN R YPHEFSGG QCQRIGIARA LILEPKLIIC DEPVSALDVS IQAQVVNLLQ QLQREMGLSL IFIAHDLAVV KHISDRVLVM YL GHAVELG TYDEVYHNPL HPYTRALMSA VPIPDPDLEK NKTIQLLEGE LPSPINPPSG CVFRTRCPIA GPECAKTRPV LEG SFRHSV SCLKVDP

UniProtKB: Oligopeptide transport ATP-binding protein OppF

-
Macromolecule #5: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 5 / Number of copies: 2 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.17 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 367365
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

+
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