7LHV

Structure of Arabidopsis thaliana sulfate transporter AtSULTR4;1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.75 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure and function of an Arabidopsis thaliana sulfate transporter.

Wang, L.Chen, K.Zhou, M.

(2021) Nat Commun 12: 4455-4455

  • DOI: https://doi.org/10.1038/s41467-021-24778-2
  • Primary Citation of Related Structures:  
    7LHV

  • PubMed Abstract: 

    Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO 4 2- ) 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 4 2- 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 4 2- is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO 4 2- are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO 4 2- transport. Glu347, which is ~7 Å from the bound SO 4 2- , 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 4 2- transport, suggesting a regulatory function of the STAS domain.


  • Organizational Affiliation

    Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sulfate transporter 4.1, chloroplastic
A, B
685Arabidopsis thalianaMutation(s): 0 
Gene Names: SULTR41At5g13550MSH12.1
Membrane Entity: Yes 
UniProt
Find proteins for Q9FY46 (Arabidopsis thaliana)
Explore Q9FY46 
Go to UniProtKB:  Q9FY46
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9FY46
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LBN
Query on LBN

Download Ideal Coordinates CCD File 
E [auth A],
J [auth B]
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
C42 H82 N O8 P
WTJKGGKOPKCXLL-VYOBOKEXSA-N
S1P
Query on S1P

Download Ideal Coordinates CCD File 
C [auth A],
F [auth A],
G [auth B],
H [auth B]
(2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate
C18 H38 N O5 P
DUYSYHSSBDVJSM-KRWOKUGFSA-N
SO4 (Subject of Investigation/LOI)
Query on SO4

Download Ideal Coordinates CCD File 
D [auth A],
I [auth B]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.75 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)United StatesDK122784
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)United StatesHL086392

Revision History  (Full details and data files)

  • Version 1.0: 2021-08-11
    Type: Initial release
  • Version 1.1: 2024-05-29
    Changes: Data collection