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5A2N

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

Replaces:  4CL4
Summary for 5A2N
Entry DOI10.2210/pdb5a2n/pdb
Related5A2O
DescriptorPROTEIN NRT1/ PTR FAMILY 6.3 (1 entity in total)
Functional Keywordstransport protein, transporter, nitrate, major facilitator superfamily, pot family, nrt1/ptr family, npf family
Biological sourceARABIDOPSIS THALIANA (THALE CRESS)
Total number of polymer chains2
Total formula weight129967.20
Authors
Parker, J.L.,Newstead, S. (deposition date: 2015-05-20, release date: 2015-06-17, Last modification date: 2024-05-08)
Primary citationParker, J.L.,Newstead, S.
Molecular Basis of Nitrate Uptake by the Plant Nitrate Transporter Nrt1.1.
Nature, 507:68-, 2014
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.7 Å)
Structure validation

237735

数据于2025-06-18公开中

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