4oh3: Difference between revisions

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-{{STRUCTURE_4oh3|  PDB=4oh3  |  SCENE=  }}
-===Crystal structure of a nitrate transporter===
-{{ABSTRACT_PUBMED_24572362}}
-==Function==
+==Crystal structure of a nitrate transporter==
-[[http://www.uniprot.org/uniprot/PTR7_ARATH PTR7_ARATH]] Dual affinity nitrate transporter. Involved in proton-dependent nitrate uptake and in the regulation of the nitrate transporter NRT2.1. Acts also as a nitrate sensor that trigger a specific signaling pathway stimulating lateral root growth and seed germination. The uptake activity is not required for sensor function. Displays an auxin transport facilitation inhibited by high nitrate concentration. Required to prevent auxin accumulation in preemerged lateral root primordia and young lateral roots when external nitrate concentration is low or null. May be involved in the basipetal transport of auxin out of the lateral root tips. Acts as a bidirectional transporter involved in root-to-shoot nitrate translocation.<ref>PMID:8453665</ref> <ref>PMID:9844028</ref> <ref>PMID:12606566</ref> <ref>PMID:12509525</ref> <ref>PMID:15319483</ref> <ref>PMID:17148611</ref> <ref>PMID:19766570</ref> <ref>PMID:19633234</ref> <ref>PMID:20627075</ref>
+<StructureSection load='4oh3' size='340' side='right'caption='[[4oh3]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4oh3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OH3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh3 OCA], [https://pdbe.org/4oh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4oh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh3 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+Crystal structure of the plant dual-affinity nitrate transporter NRT1.1.,Sun J, Bankston JR, Payandeh J, Hinds TR, Zagotta WN, Zheng N Nature. 2014 Mar 6;507(7490):73-7. doi: 10.1038/nature13074. Epub 2014 Feb 26. PMID:24572362<ref>PMID:24572362</ref>
-[[4oh3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH3 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:024572362</ref><references group="xtra"/><references/>
+</div>
-[[Category: Bankston, J R.]]
+<div class="pdbe-citations 4oh3" style="background-color:#fffaf0;"></div>
-[[Category: Hinds, T R.]]
+== References ==
-[[Category: Payandeh, J.]]
+<references/>
-[[Category: Sun, J.]]
+__TOC__
-[[Category: Zagotta, W N.]]
+</StructureSection>
-[[Category: Zheng, N.]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Major facilitator superfamily]]
+[[Category: Large Structures]]
-[[Category: Membrane]]
+[[Category: Bankston JR]]
-[[Category: Membrane protein]]
+[[Category: Hinds TR]]
-[[Category: Nitrate transporter]]
+[[Category: Payandeh J]]
-[[Category: Tranport protein]]
+[[Category: Sun J]]
+[[Category: Zagotta WN]]
+[[Category: Zheng N]]