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- EMDB-10933: Heterotetrameric structure of the rBAT-b(0,+)AT1 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-10933
TitleHeterotetrameric structure of the rBAT-b(0,+)AT1 complex
Map data
Sample
  • Complex: Heterotetrameric complex of rBAT and b(0,+)AT1
    • Protein or peptide: Neutral and basic amino acid transport protein rBAT
    • Protein or peptide: b(0,+)-type amino acid transporter 1
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM ION
KeywordsMembrane transporter Heteromeric amino acid transporter Human transporter / MEMBRANE PROTEIN
Function / homology
Function and homology information


basic amino acid transmembrane transporter activity / Defective SLC3A1 causes cystinuria (CSNU) / Defective SLC7A9 causes cystinuria (CSNU) / basic amino acid transport / broad specificity neutral L-amino acid:basic L-amino acid antiporter activity / L-cystine transmembrane transporter activity / L-cystine transport / L-glutamate transmembrane transport / aspartate transmembrane transport / amino acid transmembrane transport ...basic amino acid transmembrane transporter activity / Defective SLC3A1 causes cystinuria (CSNU) / Defective SLC7A9 causes cystinuria (CSNU) / basic amino acid transport / broad specificity neutral L-amino acid:basic L-amino acid antiporter activity / L-cystine transmembrane transporter activity / L-cystine transport / L-glutamate transmembrane transport / aspartate transmembrane transport / amino acid transmembrane transport / neutral amino acid transport / amino acid transmembrane transporter activity / Amino acid transport across the plasma membrane / neutral L-amino acid transmembrane transporter activity / Basigin interactions / antiporter activity / vacuolar membrane / amino acid transport / brush border membrane / peptide antigen binding / gene expression / protein-containing complex assembly / carbohydrate metabolic process / protein heterodimerization activity / apical plasma membrane / protein-containing complex binding / extracellular exosome / membrane / plasma membrane
Similarity search - Function
: / Amino acid/polyamine transporter I / Amino acid permease / Oligo-1,6-glucosidase, domain 2 / Alpha amylase, catalytic domain / Glycosyl hydrolase, family 13, catalytic domain / Alpha-amylase domain / Glycosyl hydrolase, all-beta / Glycoside hydrolase superfamily
Similarity search - Domain/homology
b(0,+)-type amino acid transporter 1 / Amino acid transporter heavy chain SLC3A1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsWu D / Safarian S
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Federal Ministry for Education and Research Germany
Max Planck Society Germany
CitationJournal: Proc Natl Acad Sci U S A / Year: 2020
Title: Structural basis for amino acid exchange by a human heteromeric amino acid transporter.
Authors: Di Wu / Tamara N Grund / Sonja Welsch / Deryck J Mills / Max Michel / Schara Safarian / Hartmut Michel /
Abstract: Heteromeric amino acid transporters (HATs) comprise a group of membrane proteins that belong to the solute carrier (SLC) superfamily. They are formed by two different protein components: a light ...Heteromeric amino acid transporters (HATs) comprise a group of membrane proteins that belong to the solute carrier (SLC) superfamily. They are formed by two different protein components: a light chain subunit from an SLC7 family member and a heavy chain subunit from the SLC3 family. The light chain constitutes the transport subunit whereas the heavy chain mediates trafficking to the plasma membrane and maturation of the functional complex. Mutation, malfunction, and dysregulation of HATs are associated with a wide range of pathologies or represent the direct cause of inherited and acquired disorders. Here we report the cryogenic electron microscopy structure of the neutral and basic amino acid transport complex (bAT1-rBAT) which reveals a heterotetrameric protein assembly composed of two heavy and light chain subunits, respectively. The previously uncharacterized interaction between two HAT units is mediated via dimerization of the heavy chain subunits and does not include participation of the light chain subunits. The bAT1 transporter adopts a LeuT fold and is captured in an inward-facing conformation. We identify an amino-acid-binding pocket that is formed by transmembrane helices 1, 6, and 10 and conserved among SLC7 transporters.
History
DepositionApr 27, 2020-
Header (metadata) releaseJan 20, 2021-
Map releaseJan 20, 2021-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.011
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6yup
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10933.png

Downloads & links

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Map

FileDownload / File: emd_10933.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 320 pix.
= 267.84 Å		0.84 Å/pix.
x 320 pix.
= 267.84 Å		0.84 Å/pix.
x 320 pix.
= 267.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.837 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01 / Movie #1: 0.011
Minimum - Maximum-0.0330811 - 0.07284846
Average (Standard dev.)0.0000098896735 (±0.0022957383)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 267.84 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.8370.8370.837
M x/y/z320320320
origin x/y/z0.0000.0000.000
length x/y/z267.840267.840267.840
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS320320320
D min/max/mean-0.0330.0730.000

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Supplemental data

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Half map: #2

Fileemd_10933_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_10933_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Heterotetrameric complex of rBAT and b(0,+)AT1

EntireName: Heterotetrameric complex of rBAT and b(0,+)AT1
Components
  • Complex: Heterotetrameric complex of rBAT and b(0,+)AT1
    • Protein or peptide: Neutral and basic amino acid transport protein rBAT
    • Protein or peptide: b(0,+)-type amino acid transporter 1
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM ION

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Supramolecule #1: Heterotetrameric complex of rBAT and b(0,+)AT1

SupramoleculeName: Heterotetrameric complex of rBAT and b(0,+)AT1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 / Details: 2 x rBAT 2 x b(0,+)AT1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 264.666 kDa/nm

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Macromolecule #1: Neutral and basic amino acid transport protein rBAT

MacromoleculeName: Neutral and basic amino acid transport protein rBAT / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 78.937703 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAEDKSKRDS IEMSMKGCQT NNGFVHNEDI LEQTPDPGSS TDNLKHSTRG ILGSQEPDFK GVQPYAGMPK EVLFQFSGQA RYRIPREIL FWLTVASVLV LIAATIAIIA LSPKCLDWWQ EGPMYQIYPR SFKDSNKDGN GDLKGIQDKL DYITALNIKT V WITSFYKS ...String:
MAEDKSKRDS IEMSMKGCQT NNGFVHNEDI LEQTPDPGSS TDNLKHSTRG ILGSQEPDFK GVQPYAGMPK EVLFQFSGQA RYRIPREIL FWLTVASVLV LIAATIAIIA LSPKCLDWWQ EGPMYQIYPR SFKDSNKDGN GDLKGIQDKL DYITALNIKT V WITSFYKS SLKDFRYGVE DFREVDPIFG TMEDFENLVA AIHDKGLKLI IDFIPNHTSD KHIWFQLSRT RTGKYTDYYI WH DCTHENG KTIPPNNWLS VYGNSSWHFD EVRNQCYFHQ FMKEQPDLNF RNPDVQEEIK EILRFWLTKG VDGFSLDAVK FLL EAKHLR DEIQVNKTQI PDTVTQYSEL YHDFTTTQVG MHDIVRSFRQ TMDQYSTEPG RYRFMGTEAY AESIDRTVMY YGLP FIQEA DFPFNNYLSM LDTVSGNSVY EVITSWMENM PEGKWPNWMI GGPDSSRLTS RLGNQYVNVM NMLLFTLPGT PITYY GEEI GMGNIVAANL NESYDINTLR SKSPMQWDNS SNAGFSEASN TWLPTNSDYH TVNVDVQKTQ PRSALKLYQD LSLLHA NEL LLNRGWFCHL RNDSHYVVYT RELDGIDRIF IVVLNFGEST LLNLHNMISG LPAKMRIRLS TNSADKGSKV DTSGIFL DK GEGLIFEHNT KNLLHRQTAF RDRCFVSNRA CYSSVLNILY TSC

UniProtKB: Amino acid transporter heavy chain SLC3A1

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Macromolecule #2: b(0,+)-type amino acid transporter 1

MacromoleculeName: b(0,+)-type amino acid transporter 1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 53.515992 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGDTGLRKRR EDEKSIQSQE PKTTSLQKEL GLISGISIIV GTIIGSGIFV SPKSVLSNTE AVGPCLIIWA ACGVLATLGA LCFAELGTM ITKSGGEYPY LMEAYGPIPA YLFSWASLIV IKPTSFAIIC LSFSEYVCAP FYVGCKPPQI VVKCLAAAAI L FISTVNSL ...String:
MGDTGLRKRR EDEKSIQSQE PKTTSLQKEL GLISGISIIV GTIIGSGIFV SPKSVLSNTE AVGPCLIIWA ACGVLATLGA LCFAELGTM ITKSGGEYPY LMEAYGPIPA YLFSWASLIV IKPTSFAIIC LSFSEYVCAP FYVGCKPPQI VVKCLAAAAI L FISTVNSL SVRLGSYVQN IFTAAKLVIV AIIIISGLVL LAQGNTKNFD NSFEGAQLSV GAISLAFYNG LWAYDGWNQL NY ITEELRN PYRNLPLAII IGIPLVTACY ILMNVSYFTV MTATELLQSQ AVAVTFGDRV LYPASWIVPL FVAFSTIGAA NGT CFTAGR LIYVAGREGH MLKVLSYISV RRLTPAPAII FYGIIATIYI IPGDINSLVN YFSFAAWLFY GLTILGLIVM RFTR KELER PIKVPVVIPV LMTLISVFLV LAPIISKPTW EYLYCVLFIL SGLLFYFLFV HYKFGWAQKI SKPITMHLQM LMEVV PPEE DPE

UniProtKB: b(0,+)-type amino acid transporter 1

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Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 8 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #4: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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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

Concentration2.5 mg/mL
BufferpH: 7.5
Component:
ConcentrationName
25.0 mMTris
150.0 mMNaCl
0.1 % (w/V)Digitonin
GridModel: C-flat-1.2/1.3 4C / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 92789
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
FSC plot (resolution estimation)

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