Crystal structure of the plant dual-affinity nitrate transporter NRT1.1

Ji Sun, John R. Bankston, Jian Payandeh, Thomas R. Hinds, William N. Zagotta and Ning Zheng ()
Additional contact information
Ji Sun: Box 357280, University of Washington
John R. Bankston: Box 357290, University of Washington
Jian Payandeh: Box 357280, University of Washington
Thomas R. Hinds: Box 357280, University of Washington
William N. Zagotta: Box 357290, University of Washington
Ning Zheng: Box 357280, University of Washington

Nature, 2014, vol. 507, issue 7490, 73-77

Abstract: Abstract Nitrate is a primary nutrient for plant growth, but its levels in soil can fluctuate by several orders of magnitude. Previous studies have identified Arabidopsis NRT1.1 as a dual-affinity nitrate transporter that can take up nitrate over a wide range of concentrations. The mode of action of NRT1.1 is controlled by phosphorylation of a key residue, Thr 101; however, how this post-translational modification switches the transporter between two affinity states remains unclear. Here we report the crystal structure of unphosphorylated NRT1.1, which reveals an unexpected homodimer in the inward-facing conformation. In this low-affinity state, the Thr 101 phosphorylation site is embedded in a pocket immediately adjacent to the dimer interface, linking the phosphorylation status of the transporter to its oligomeric state. Using a cell-based fluorescence resonance energy transfer assay, we show that functional NRT1.1 dimerizes in the cell membrane and that the phosphomimetic mutation of Thr 101 converts the protein into a monophasic high-affinity transporter by structurally decoupling the dimer. Together with analyses of the substrate transport tunnel, our results establish a phosphorylation-controlled dimerization switch that allows NRT1.1 to uptake nitrate with two distinct affinity modes.

Date: 2014
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DOI: 10.1038/nature13074

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