5A2O

Crystal structure of the nitrate transporter NRT1.1 from Arabidopsis thaliana in complex with nitrate.

Replaces:  4CL5

Summary for 5A2O

• Entry DOI: 10.2210/pdb5a2o/pdb
• Related: 5A2N
• Descriptor: NITRATE TRANSPORTER 1.1, NITRATE ION (2 entities in total)
• Functional Keywords: transport protein, transporter, nitrate, mfs, pot family, nrt1/ptr family, npf family, mfs transporter
• Biological source: ARABIDOPSIS THALIANA (THALE CRESS)
• Total number of polymer chains: 2
• Total formula weight: 130091.21

Authors

Parker, J.L.,Newstead, S. (deposition date: 2015-05-20, release date: 2015-06-17, Last modification date: 2024-05-08)

Primary citation

Parker, J.L.,Newstead, S.
Molecular Basis of Nitrate Uptake by the Plant Nitrate Transporter Nrt1.1.
Nature, 507:68-, 2014

PubMed Abstract: The NRT1/PTR family of proton-coupled transporters are responsible for nitrogen assimilation in eukaryotes and bacteria through the uptake of peptides. However, in most plant species members of this family have evolved to transport nitrate as well as additional secondary metabolites and hormones. In response to falling nitrate levels, NRT1.1 is phosphorylated on an intracellular threonine that switches the transporter from a low-affinity to high-affinity state. Here we present both the apo and nitrate-bound crystal structures of Arabidopsis thaliana NRT1.1, which together with in vitro binding and transport data identify a key role for His 356 in nitrate binding. Our data support a model whereby phosphorylation increases structural flexibility and in turn the rate of transport. Comparison with peptide transporters further reveals how the NRT1/PTR family has evolved to recognize diverse nitrogenous ligands, while maintaining elements of a conserved coupling mechanism within this superfamily of nutrient transporters.

PubMed: 24572366
DOI: 10.1038/NATURE13116

Experimental method

X-RAY DIFFRACTION (3.71 Å)