5A2O
Crystal structure of the nitrate transporter NRT1.1 from Arabidopsis thaliana in complex with nitrate.
「4CL5」から置き換えられました5A2O の概要
| エントリーDOI | 10.2210/pdb5a2o/pdb |
| 関連するPDBエントリー | 5A2N |
| 分子名称 | NITRATE TRANSPORTER 1.1, NITRATE ION (2 entities in total) |
| 機能のキーワード | transport protein, transporter, nitrate, mfs, pot family, nrt1/ptr family, npf family, mfs transporter |
| 由来する生物種 | ARABIDOPSIS THALIANA (THALE CRESS) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 130091.21 |
| 構造登録者 | |
| 主引用文献 | Parker, 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: 24572366DOI: 10.1038/NATURE13116 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.71 Å) |
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