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- EMDB-30938: Human bile salt exporter ABCB11 in complex with taurocholate -

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Basic information

Entry
Database: EMDB / ID: EMD-30938
TitleHuman bile salt exporter ABCB11 in complex with taurocholate
Map data
Sample
  • Complex: human ABCB11 in complex with taurocholate
    • Protein or peptide: Bile salt export pump
  • Ligand: TAUROCHOLIC ACID
KeywordsABC transporter / liver / membrane protein
Function / homology
Function and homology information


canalicular bile acid transmembrane transporter activity / positive regulation of bile acid secretion / Defective ABCB11 causes PFIC2 and BRIC2 / canalicular bile acid transport / intracellular canaliculus / regulation of fatty acid beta-oxidation / xenobiotic export from cell / : / ABC-type bile acid transporter activity / bile acid biosynthetic process ...canalicular bile acid transmembrane transporter activity / positive regulation of bile acid secretion / Defective ABCB11 causes PFIC2 and BRIC2 / canalicular bile acid transport / intracellular canaliculus / regulation of fatty acid beta-oxidation / xenobiotic export from cell / : / ABC-type bile acid transporter activity / bile acid biosynthetic process / phospholipid homeostasis / xenobiotic transmembrane transport / intercellular canaliculus / bile acid metabolic process / bile acid transmembrane transporter activity / Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate / ABC-type xenobiotic transporter activity / bile acid and bile salt transport / lipid homeostasis / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / Recycling of bile acids and salts / xenobiotic metabolic process / cholesterol homeostasis / fatty acid metabolic process / recycling endosome / transmembrane transport / recycling endosome membrane / endosome / protein ubiquitination / apical plasma membrane / cell surface / ATP hydrolysis activity / extracellular exosome / ATP binding / plasma membrane
Similarity search - Function
Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / 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. ...Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / 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
Bile salt export pump
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.66 Å
AuthorsWang L / How WT
Funding support China, 1 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2019YFA0508500 China
CitationJournal: Cell Res / Year: 2022
Title: Structures of human bile acid exporter ABCB11 reveal a transport mechanism facilitated by two tandem substrate-binding pockets.
Authors: Liang Wang / Wen-Tao Hou / Jie Wang / Da Xu / Cong Guo / Linfeng Sun / Ke Ruan / Cong-Zhao Zhou / Yuxing Chen /
History
DepositionFeb 1, 2021-
Header (metadata) releaseFeb 9, 2022-
Map releaseFeb 9, 2022-
UpdateJun 5, 2024-
Current statusJun 5, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.4
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.4
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7e1a
  • Surface level: 0.4
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30938.png

Downloads & links

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Map

FileDownload / File: emd_30938.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 216 pix.
= 228.96 Å		1.06 Å/pix.
x 216 pix.
= 228.96 Å		1.06 Å/pix.
x 216 pix.
= 228.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 0.332 / Movie #1: 0.4
Minimum - Maximum-2.1638567 - 3.2226255
Average (Standard dev.)0.005914309 (±0.07871399)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions216216216
Spacing216216216
CellA=B=C: 228.95999 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z216216216
origin x/y/z0.0000.0000.000
length x/y/z228.960228.960228.960
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ256256256
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS216216216
D min/max/mean-2.1643.2230.006

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Supplemental data

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Sample components

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Entire : human ABCB11 in complex with taurocholate

EntireName: human ABCB11 in complex with taurocholate
Components
  • Complex: human ABCB11 in complex with taurocholate
    • Protein or peptide: Bile salt export pump
  • Ligand: TAUROCHOLIC ACID

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Supramolecule #1: human ABCB11 in complex with taurocholate

SupramoleculeName: human ABCB11 in complex with taurocholate / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 150 KDa

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Macromolecule #1: Bile salt export pump

MacromoleculeName: Bile salt export pump / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 146.557391 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSDSVILRSI KKFGEENDGF ESDKSYNNDK KSRLQDEKKG DGVRVGFFQL FRFSSSTDIW LMFVGSLCAF LHGIAQPGVL LIFGTMTDV FIDYDVELQE LQIPGKACVN NTIVWTNSSL NQNMTNGTRC GLLNIESEMI KFASYYAGIA VAVLITGYIQ I CFWVIAAA ...String:
MSDSVILRSI KKFGEENDGF ESDKSYNNDK KSRLQDEKKG DGVRVGFFQL FRFSSSTDIW LMFVGSLCAF LHGIAQPGVL LIFGTMTDV FIDYDVELQE LQIPGKACVN NTIVWTNSSL NQNMTNGTRC GLLNIESEMI KFASYYAGIA VAVLITGYIQ I CFWVIAAA RQIQKMRKFY FRRIMRMEIG WFDCNSVGEL NTRFSDDINK INDAIADQMA LFIQRMTSTI CGFLLGFFRG WK LTLVIIS VSPLIGIGAA TIGLSVSKFT DYELKAYAKA GVVADEVISS MRTVAAFGGE KREVERYEKN LVFAQRWGIR KGI VMGFFT GFVWCLIFLC YALAFWYGST LVLDEGEYTP GTLVQIFLSV IVGALNLGNA SPCLEAFATG RAAATSIFET IDRK PIIDC MSEDGYKLDR IKGEIEFHNV TFHYPSRPEV KILNDLNMVI KPGEMTALVG PSGAGKSTAL QLIQRFYDPC EGMVT VDGH DIRSLNIQWL RDQIGIVEQE PVLFSTTIAE NIRYGREDAT MEDIVQAAKE ANAYNFIMDL PQQFDTLVGE GGGQMS GGQ KQRVAIARAL IRNPKILLLD MATSALDNES EAMVQEVLSK IQHGHTIISV AHRLSTVRAA DTIIGFEHGT AVERGTH EE LLERKGVYFT LVTLQSQGNQ ALNEEDIKDA TEDDMLARTF SRGSYQDSLR ASIRQRSKSQ LSYLVHEPPL AVVDHKST Y EEDRKDKDIP VQEEVEPAPV RRILKFSAPE WPYMLVGSVG AAVNGTVTPL YAFLFSQILG TFSIPDKEEQ RSQINGVCL LFVAMGCVSL FTQFLQGYAF AKSGELLTKR LRKFGFRAML GQDIAWFDDL RNSPGALTTR LATDASQVQG AAGSQIGMIV NSFTNVTVA MIIAFSFSWK LSLVILCFFP FLALSGATQT RMLTGFASRD KQALEMVGQI TNEALSNIRT VAGIGKERRF I EALETELE KPFKTAIQKA NIYGFCFAFA QCIMFIANSA SYRYGGYLIS NEGLHFSYVF RVISAVVLSA TALGRAFSYT PS YAKAKIS AARFFQLLDR QPPISVYNTA GEKWDNFQGK IDFVDCKFTY PSRPDSQVLN GLSVSISPGQ TLAFVGSSGC GKS TSIQLL ERFYDPDQGK VMIDGHDSKK VNVQFLRSNI GIVSQEPVLF ACSIMDNIKY GDNTKEIPME RVIAAAKQAQ LHDF VMSLP EKYETNVGSQ GSQLSRGEKQ RIAIARAIVR DPKILLLDEA TSALDTESEK TVQVALDKAR EGRTCIVIAH RLSTI QNAD IIAVMAQGVV IEKGTHEELM AQKGAYYKLV TTGSPIS

UniProtKB: Bile salt export pump

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Macromolecule #2: TAUROCHOLIC ACID

MacromoleculeName: TAUROCHOLIC ACID / type: ligand / ID: 2 / Number of copies: 1 / Formula: TCH
Molecular weightTheoretical: 515.703 Da
Chemical component information

ChemComp-TCH:
TAUROCHOLIC ACID

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration5.8 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: DIFFRACTION
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2147192
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.66 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.2) / Number images used: 170023
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: RANDOM ASSIGNMENT
FSC plot (resolution estimation)

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