[English] 日本語
Yorodumi
- EMDB-55024: Cryo-EM structure of the closed-closed dextran utilisome (BT3087-... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-55024
TitleCryo-EM structure of the closed-closed dextran utilisome (BT3087-BT3090), with GHdex D297A E360A catalytic inactivation, with bound IMO4, IMO6 and IMO8
Map dataA map of the dextran utilisome in the closed-closed (CC) conformation
Sample
  • Complex: Dextran utilisome of Bacteroides thetaiotaomicron, with a catalytic-inactive GHdex, in complex with dextran.
    • Protein or peptide: SusC homolog
    • Protein or peptide: SusD homolog
    • Protein or peptide: BT3088 (SGBPdex)
    • Protein or peptide: Cycloisomaltooligosaccharide glucanotransferase
Keywordsdextran / dextranase / SusD / SGBP / Bacteroides / GH / glycoside hydrolase / utilisome / GH66 / TBDT / MEMBRANE PROTEIN
Function / homology
Function and homology information


cell outer membrane
Similarity search - Function
SusE outer membrane protein / SusE outer membrane protein / Glycosyl hydrolase family 66 / Glycosyl hydrolase family 66 / CarboxypepD_reg-like domain / TonB-dependent outer membrane protein, SusC/RagA / TonB-dependent outer membrane protein SusC/RagA, conserved site / SusD-like, N-terminal / Starch-binding associating with outer membrane / RagB/SusD domain ...SusE outer membrane protein / SusE outer membrane protein / Glycosyl hydrolase family 66 / Glycosyl hydrolase family 66 / CarboxypepD_reg-like domain / TonB-dependent outer membrane protein, SusC/RagA / TonB-dependent outer membrane protein SusC/RagA, conserved site / SusD-like, N-terminal / Starch-binding associating with outer membrane / RagB/SusD domain / SusD family / Carboxypeptidase-like, regulatory domain superfamily / TonB-dependent receptor (TBDR) proteins profile. / Vitamin B12 transporter BtuB-like / TonB-dependent receptor, plug domain superfamily / TonB-dependent receptor, plug domain / TonB-dependent Receptor Plug Domain / TonB-dependent receptor-like, beta-barrel domain superfamily / Glycosyl hydrolase, all-beta / Prokaryotic membrane lipoprotein lipid attachment site profile. / Tetratricopeptide-like helical domain superfamily / Glycoside hydrolase superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
SusC homolog / SusD homolog / SusE outer membrane protein domain-containing protein / Cycloisomaltooligosaccharide glucanotransferase
Similarity search - Component
Biological speciesBacteroides thetaiotaomicron VPI-5482 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.5 Å
AuthorsFeasey M / Basle A / van den Berg B
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Wellcome Trust214222/Z/18/Z United Kingdom
CitationJournal: J Struct Biol X / Year: 2026
Title: Structural and functional characterisation of the dextran utilisome from Bacteroides thetaiotaomicron
Authors: Feasey M / Silale A / Basle A / van den Berg B
History
DepositionSep 5, 2025-
Header (metadata) releaseJul 29, 2026-
Map releaseJul 29, 2026-
UpdateJul 29, 2026-
Current statusJul 29, 2026Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_55024.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationA map of the dextran utilisome in the closed-closed (CC) conformation
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 400 pix.
= 332.4 Å
0.83 Å/pix.
x 400 pix.
= 332.4 Å
0.83 Å/pix.
x 400 pix.
= 332.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.831 Å
Density
Contour LevelBy AUTHOR: 0.015
Minimum - Maximum-0.06966317 - 0.18863633
Average (Standard dev.)0.00044467277 (±0.006118888)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 332.4 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: Half map A

Fileemd_55024_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map B

Fileemd_55024_half_map_2.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Dextran utilisome of Bacteroides thetaiotaomicron, with a catalyt...

EntireName: Dextran utilisome of Bacteroides thetaiotaomicron, with a catalytic-inactive GHdex, in complex with dextran.
Components
  • Complex: Dextran utilisome of Bacteroides thetaiotaomicron, with a catalytic-inactive GHdex, in complex with dextran.
    • Protein or peptide: SusC homolog
    • Protein or peptide: SusD homolog
    • Protein or peptide: BT3088 (SGBPdex)
    • Protein or peptide: Cycloisomaltooligosaccharide glucanotransferase

-
Supramolecule #1: Dextran utilisome of Bacteroides thetaiotaomicron, with a catalyt...

SupramoleculeName: Dextran utilisome of Bacteroides thetaiotaomicron, with a catalytic-inactive GHdex, in complex with dextran.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Co-purified complex from B. theta with a His-tag on SusDdex. Dextran substrate added prior to vitrification.
Source (natural)Organism: Bacteroides thetaiotaomicron VPI-5482 (bacteria) / Strain: TDK- / Location in cell: Outer membrane
Molecular weightTheoretical: 580 KDa

-
Macromolecule #1: SusC homolog

MacromoleculeName: SusC homolog / type: protein_or_peptide / ID: 1 / Details: Co-purified via His6-tag on BT3089 (SusDdex) / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bacteroides thetaiotaomicron VPI-5482 (bacteria)
Molecular weightTheoretical: 110.591242 KDa
SequenceString: MEQSIKSKGF EHRLLLIMWG LLLSLSAFAQ QITVKGHVVD ATGEPVIGAS VIEGKSTNGT ITDIDGNFSL NVSANSALTI SFVGYKTQT VSVNGKTALK VTLQEDTEVL DEVVVVGYGT MKKSDLTGAV SSVGVKDIKD SPVANIGQAM QGKVSGVQII D AGKPGDNV ...String:
MEQSIKSKGF EHRLLLIMWG LLLSLSAFAQ QITVKGHVVD ATGEPVIGAS VIEGKSTNGT ITDIDGNFSL NVSANSALTI SFVGYKTQT VSVNGKTALK VTLQEDTEVL DEVVVVGYGT MKKSDLTGAV SSVGVKDIKD SPVANIGQAM QGKVSGVQII D AGKPGDNV TIKIRGLGTI NNSNPLVVID GIPTDLGLSS LNMADVERVD VLKDASATAI YGSRGANGVV MITSKRGAEG AG KVTVNAN WAIQNATKVP DMLNAAQYAA LSNDMLSNND DNTNPYWADP SSLGKGTNWL DEMLRTGVKQ SYSVSYSGGT EKA HYYVSG GFLDQSGIVK SVNYRRFNFQ ANSDAQVNKW LKFTTNLTFS TDVKEGGTYS IGDAMKALPT QPVKNDDGSW SGPG QEAQW YGSIRNPIGT LHMMTNETKG YNFLANITGE ITFTKWLKLK STFGYDAKFW FADNFTPAYD WKPNPVEESS RYKSD NKSF TYLWDNYFVF DHTFAKKHRV GVMAGSSAQW NNYDYLNAQK NIFMFDNIHE MDNGEKMYSL GGSQSDWALL SLMARL NYS YEDKYLLTAT VRRDGSSRFG KNNRWGTFPS VSLAWRVSQE DWFPKDNFLM NDLKLRVGYG VTGNQEIGNY GFVASYN TG VYPFGNNNST ALVSTTLSNP NIHWEEVRQA NFGVDMSLFD SRVSLSLDAY IKNTNDMLVK ASIPITSGFE DTTETFTN A GKMRNKGVEM TLRTINLKGI FSWESALTAT YNKNEILDLN SETPMFINQI GNSYVTMLKA GYPINVFYGY VTDGLFQNW GEVNRHATQP GAAPGDIRFR DLNNDGVIND EDRTILGNPN PNWFFSLSNN LSYKGWELSV FLQGVAGNKI YNANNVDNEG MAAAYNQTT AVLNRWTGEG TSYSMPRAIW GDPNQNCRVS DRFVENGSYL RLKNITLSYT LPKKWLQKIQ LENARISFSC E NVATITRY SGFDPEVDVN GIDSSRYPIS RTFSMGLNFN F

UniProtKB: SusC homolog

-
Macromolecule #2: SusD homolog

MacromoleculeName: SusD homolog / type: protein_or_peptide / ID: 2 / Details: "AAAAHHHHHHH" tag added through genomic cloning / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bacteroides thetaiotaomicron VPI-5482 (bacteria)
Molecular weightTheoretical: 56.873871 KDa
Recombinant expressionOrganism: Bacteroides thetaiotaomicron VPI-5482 (bacteria)
SequenceString: MKKKLTFIMI LAVLALTSCS DFLDKYPKYG VDPESEVTNE IAVALTTACY KTLQSSNMYN QRLWSLDILA GNSEVGAGGG TDGLETVQA ANFIAQSDNG FALYVWRSPW VGIGRCNIVL SNLPSAAISD EIKDRCMGEA YFLRAHYYYI LVRLYGGVPL R LQPFEPGQ ...String:
MKKKLTFIMI LAVLALTSCS DFLDKYPKYG VDPESEVTNE IAVALTTACY KTLQSSNMYN QRLWSLDILA GNSEVGAGGG TDGLETVQA ANFIAQSDNG FALYVWRSPW VGIGRCNIVL SNLPSAAISD EIKDRCMGEA YFLRAHYYYI LVRLYGGVPL R LQPFEPGQ STDIARNTVD EVYAQILSDC KNAVDMLPPK SSYGENDKGR ACKEAAMAML ADIYLTLAPN HRDYYNEVVT LC DQITAMG YDLSQCKYAD NFDATINNGA ESLFEVQYSG STEYDFWGGD NQSSWLSTFM GPRNSGMVAG AYGWNLPTEE FIK EYEAGD LRKDVTVLYQ GCPAFDGMEY RRSWSNTGYN VRKFLVSKTV SPEYNTNPNN FVVYRYADVL LKKAEALNEL GHPD QAAAP LNIVRQRAGL ADVPTTLNQE TMREKIIHER RMELAFEGHR WFDMIRINNG NYAIEFLKSI GKNQVTKERL LLPIP QTEM DSNNLMTQNP GYAAAAHHHH HH

UniProtKB: SusD homolog

-
Macromolecule #3: BT3088 (SGBPdex)

MacromoleculeName: BT3088 (SGBPdex) / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bacteroides thetaiotaomicron VPI-5482 (bacteria) / Strain: TDK-
Molecular weightTheoretical: 56.086352 KDa
SequenceString: MKKYIYQILC SLFIGGAMVS CAEDYMETDK GHDTLTLTVN QQEIVLNEKN HTQEALTLSW TTGTNYGSGN RISYTLEIAK AGTDFARAY SVDLGTGTYQ WTKKTEELNQ FLNTQLGVGY AEKVSLEARI TATVAGMEEK EQRATVALDV TTYQPVTPTL Y LIGEAAPN ...String:
MKKYIYQILC SLFIGGAMVS CAEDYMETDK GHDTLTLTVN QQEIVLNEKN HTQEALTLSW TTGTNYGSGN RISYTLEIAK AGTDFARAY SVDLGTGTYQ WTKKTEELNQ FLNTQLGVGY AEKVSLEARI TATVAGMEEK EQRATVALDV TTYQPVTPTL Y LIGEAAPN GWSADQATPM ERTDNGQFTW TGKLNTGVFK FITTLGEFLP SYNRDAAAGE ELRLIYRTSG DEPDEPFTVS KE ATYIVKV DLLDLTMTMT ETENIGWRFE EFYIVGSFTG DNGWGFEALS KDAVQMNLFH YGAVIPWKAD GDFKFTSVTD FGQ SDAFFH PTEGNAPYTS TSVVLGGEDN KWQMKESECG KAYKVLFLTA KGKEKMLMRP FTPYEGLYLV GDATPNGWSI DNAT PMAKS ADSPYIFTWS GTLNTGEMKI SCDKQSDWNG DWLMADKSGK APTGEVETAL FTSKTDAELK NMYPDTDLGS LDNKW NIQE AGSYRITIDQ LKETISIVKQ

UniProtKB: SusE outer membrane protein domain-containing protein

-
Macromolecule #4: Cycloisomaltooligosaccharide glucanotransferase

MacromoleculeName: Cycloisomaltooligosaccharide glucanotransferase / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bacteroides thetaiotaomicron VPI-5482 (bacteria) / Strain: TDK-
Molecular weightTheoretical: 66.515367 KDa
Recombinant expressionOrganism: Bacteroides thetaiotaomicron VPI-5482 (bacteria)
SequenceString: MKKIIYLVAA FLCLSCSDDH ESNPQNGGAS GSVTEVTPVT SDLCVELTTD KAFYKPNETV TFTAADALPA GTKVRYRLLG EIVGEEPVS GTNWTWKAPS TDFKGYMAEL YRQENGTDVI VGTIAVDVSS HPARFPRYGF VADFDGVKTE EKTLEEMAYL N RHHINWVQ ...String:
MKKIIYLVAA FLCLSCSDDH ESNPQNGGAS GSVTEVTPVT SDLCVELTTD KAFYKPNETV TFTAADALPA GTKVRYRLLG EIVGEEPVS GTNWTWKAPS TDFKGYMAEL YRQENGTDVI VGTIAVDVSS HPARFPRYGF VADFDGVKTE EKTLEEMAYL N RHHINWVQ FQDWHNKHHW PLGGTRTQLD EEYLDIANRP VHTSSVKNYI KAQQHFGMKS MFYNLCFGAL KDAASDGVKE EW YLFKDAS HTTKDSHDLP SGWKSNIYLV DPSDKEWQQY MAERNDDVYA NFAFDGYQIA QLGKRGTLYN YNGTPVNLRE GYA SFIEAM KQAHPDKSLV MNAVSRYGAR QIGETGKVDF FYNAMWADEA DFTHLKAVLY ENGVYGNNQL NTVFAAYMNY NKAD HRGEF NTAGILLTDA VMFALGGSHL ELGGDHMLCK EYFPNDNLTM SEELKTAMVH YYDFLTSYQN LLRDGGTENS IAMNC TNGE MKLNVWPPKL GSVTTYAKQV DGKQVVHLLN FSQANSLSWR DVDGTMPEPA LITKATLQMN LPAKVNKLWV ASPDVH GGA LQELAFTQEN GVVSFTLPAL KYWTMIVAE

UniProtKB: Cycloisomaltooligosaccharide glucanotransferase

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration7.5 mg/mL
BufferpH: 7.5 / Component:
ConcentrationName
10.0 mMHEPES
100.0 mMNaCl

Details: pH 7.5 Residual LMNG (unknown %) after SEC without detergent
GridModel: UltrAuFoil R2/2 / Material: GOLD / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 180 sec. / Pretreatment - Atmosphere: AIR
Details: 20mA, 90 seconds per side (total 180 sec). Grids were then PEGylated: After glow discharge, grids were imported into an anaerobic glovebox and submerged in ethanol containing 5mM ...Details: 20mA, 90 seconds per side (total 180 sec). Grids were then PEGylated: After glow discharge, grids were imported into an anaerobic glovebox and submerged in ethanol containing 5mM hexa(ethylene glycol)mono-11-mercaptoundecyl ether for ~24 hours. Prior to use, grids were removed from the glovebox and successively washed three times in fresh aliquots of ethanol and left to air dry.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
Details: Added dextran 1.5 & 5 (0.5 mM) and Fluorinated Octyl Maltoside at 0.05% (CMC).
DetailsEluted from a single peak on a Superose 6 Increase 10/300 GL column

-
Electron microscopy

MicroscopeTFS KRIOS
DetailsKrios recollection of a grid previously collected Glacios grid. Grid squares previously collected were excluded.
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 23.1 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 4556980 / Details: Blob picked
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Details: Pre-deposition X-ray PDB models, cryoEM PDB 8AA4, and Alphafold2
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 116104
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final 3D classificationNumber classes: 10
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