Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1.

Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1.
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DOI:
10.1038/nature13116
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发表时间:
2014-03-06
期刊:
影响因子:
64.8
通讯作者:
Newstead, Simon
Newstead, Simon
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Parker, Joanne L.;Newstead, Simon

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质子偶联转运蛋白NRT 1/PTR家族通过肽的摄取负责真核生物和细菌中的氮同化。然而,在大多数植物物种中,这个家族的成员已经进化到运输硝酸盐以及额外的次级代谢产物和激素。为了响应硝酸盐水平的下降,NRT1.1在细胞内苏氨酸上磷酸化,从而将转运蛋白从低亲和力状态切换到高亲和力状态。在这里,我们提出了拟南芥NRT1.1的载脂蛋白和硝酸盐结合的晶体结构,它与体外结合和运输数据一起确定了His 356在硝酸盐结合中的关键作用。我们的数据支持一个模型,即磷酸化增加了结构的灵活性,从而提高了运输速度。与肽转运蛋白的比较进一步揭示了NRT 1/PTR家族如何进化以识别不同的含氮配体,同时保持营养转运蛋白超家族中保守偶联机制的元素。
The NRT1/PTR family of proton-coupled transporters are responsible for nitrogen assimilation in eukaryotes and bacteria through the uptake of peptides. However, in the majority of 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 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 His356 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, whilst maintaining elements of a conserved coupling mechanism within this superfamily of nutrient transporters.
DOI: 10.1107/s090744491003982x
发表时间: 2011-04
期刊: Acta crystallographica. Section D, Biological crystallography
影响因子: --
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Evans PR
通讯作者: Evans PR
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发表时间: 2008-01-01
期刊: NATURE PROTOCOLS
影响因子: 14.8
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期刊: PLANT CELL
影响因子: 11.6
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通讯作者: Tsay, YF