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- PDB-7lhv: Structure of Arabidopsis thaliana sulfate transporter AtSULTR4;1 -

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Basic information

Entry
Database: PDB / ID: 7lhv
TitleStructure of Arabidopsis thaliana sulfate transporter AtSULTR4;1
ComponentsSulfate transporter 4.1, chloroplastic
KeywordsTRANSPORT PROTEIN / Sulfate transport / SLC26 / MEMBRANE PROTEIN
Function / homology
Function and homology information


: / chloroplast membrane / secondary active sulfate transmembrane transporter activity / symporter activity / plasma membrane => GO:0005886
Similarity search - Function
Sulphate anion transporter, conserved site / SLC26A transporters signature. / SLC26A/SulP transporter / SLC26A/SulP transporter domain / Sulfate permease family / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily
Similarity search - Domain/homology
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / Chem-S1P / Sulfate transporter 4.1, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.75 Å
AuthorsWang, L. / Chen, K. / Zhou, M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)DK122784 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL086392 United States
CitationJournal: Nat Commun / Year: 2021
Title: Structure and function of an Arabidopsis thaliana sulfate transporter.
Authors: Lie Wang / Kehan Chen / Ming Zhou /
Abstract: Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO) and are essential for plant growth; however, our understanding of their structures and functions remains ...Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO) and are essential for plant growth; however, our understanding of their structures and functions remains inadequate. Here we present the structure of a SULTR from Arabidopsis thaliana, AtSULTR4;1, in complex with SO at an overall resolution of 2.8 Å. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO transport. Glu347, which is ~7 Å from the bound SO, is required for H-driven transport. The cytosolic STAS domain interacts with transmembrane domains, and deletion of the STAS domain or mutations to the interface compromises dimer formation and reduces SO transport, suggesting a regulatory function of the STAS domain.
History
DepositionJan 26, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 11, 2021Provider: repository / Type: Initial release

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Structure visualization

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Assembly

Deposited unit
A: Sulfate transporter 4.1, chloroplastic
B: Sulfate transporter 4.1, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,56610
Polymers150,3362
Non-polymers3,2308
Water362
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Sulfate transporter 4.1, chloroplastic / AST82


Mass: 75168.164 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: SULTR4;1, At5g13550, MSH12.1, T6I14_80 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9FY46
#2: Chemical
ChemComp-S1P / (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate / sphingosine 1-phosphate / Sphingosine-1-phosphate


Mass: 379.472 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C18H38NO5P
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-LBN / 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / (2R)-2-[(9Z)-9-Octadecenoyloxy]-3-(palmitoyloxy)propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C42H82NO8P / Comment: phospholipid*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Sulfate transporter 4;1 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Molecular weightValue: 0.070 MDa / Experimental value: NO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Trichoplusia ni (cabbage looper)
Buffer solutionpH: 6
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.19.1_4122: / Classification: refinement
CTF correctionType: NONE
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 2.75 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 838096 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039312
ELECTRON MICROSCOPYf_angle_d0.50612646
ELECTRON MICROSCOPYf_dihedral_angle_d5.6321372
ELECTRON MICROSCOPYf_chiral_restr0.041488
ELECTRON MICROSCOPYf_plane_restr0.0041548

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