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| - | ==Crystal structure of the nitrate transporter NRT1.1 from Arabidopsis thaliana in complex with nitrate.==
| + | #REDIRECT [[5a2o]] This PDB entry is obsolete and replaced by 5a2o |
| - | <StructureSection load='4cl5' size='340' side='right' caption='[[4cl5]], [[Resolution|resolution]] 3.71Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4cl5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CL5 FirstGlance]. <br>
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| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene><br>
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| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cl4|4cl4]]</td></tr>
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| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cl5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cl5 RCSB], [http://www.ebi.ac.uk/pdbsum/4cl5 PDBsum]</span></td></tr>
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| - | <table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1.,Parker JL, Newstead S Nature. 2014 Mar 6;507(7490):68-72. doi: 10.1038/nature13116. Epub 2014 Feb 26. PMID:24572366<ref>PMID:24572366</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Arath]]
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| - | [[Category: Newstead, S.]]
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| - | [[Category: Parker, J L.]]
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| - | [[Category: Mf]]
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| - | [[Category: Mfs transporter]]
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| - | [[Category: Npf family]]
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| - | [[Category: Nrt1/ptr family]]
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| - | [[Category: Pot family]]
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| - | [[Category: Transport protein]]
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