5a2o

From Proteopedia

(Difference between revisions)

Revision as of 17:07, 22 March 2017

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

Structural highlights

5a2o is a 2 chain structure. This structure supersedes the now removed PDB entry 4cl5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5a2n
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

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.

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^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tsay YF, Schroeder JI, Feldmann KA, Crawford NM. The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-inducible nitrate transporter. Cell. 1993 Mar 12;72(5):705-13. PMID:8453665
↑ Wang R, Liu D, Crawford NM. The Arabidopsis CHL1 protein plays a major role in high-affinity nitrate uptake. Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):15134-9. PMID:9844028
↑ Liu KH, Tsay YF. Switching between the two action modes of the dual-affinity nitrate transporter CHL1 by phosphorylation. EMBO J. 2003 Mar 3;22(5):1005-13. PMID:12606566 doi:http://dx.doi.org/10.1093/emboj/cdg118
↑ Guo FQ, Young J, Crawford NM. The nitrate transporter AtNRT1.1 (CHL1) functions in stomatal opening and contributes to drought susceptibility in Arabidopsis. Plant Cell. 2003 Jan;15(1):107-17. PMID:12509525
↑ Munos S, Cazettes C, Fizames C, Gaymard F, Tillard P, Lepetit M, Lejay L, Gojon A. Transcript profiling in the chl1-5 mutant of Arabidopsis reveals a role of the nitrate transporter NRT1.1 in the regulation of another nitrate transporter, NRT2.1. Plant Cell. 2004 Sep;16(9):2433-47. Epub 2004 Aug 19. PMID:15319483 doi:http://dx.doi.org/10.1105/tpc.104.024380
↑ Remans T, Nacry P, Pervent M, Filleur S, Diatloff E, Mounier E, Tillard P, Forde BG, Gojon A. The Arabidopsis NRT1.1 transporter participates in the signaling pathway triggering root colonization of nitrate-rich patches. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):19206-11. Epub 2006 Dec 5. PMID:17148611 doi:http://dx.doi.org/10.1073/pnas.0605275103
↑ Ho CH, Lin SH, Hu HC, Tsay YF. CHL1 functions as a nitrate sensor in plants. Cell. 2009 Sep 18;138(6):1184-94. doi: 10.1016/j.cell.2009.07.004. PMID:19766570 doi:http://dx.doi.org/10.1016/j.cell.2009.07.004
↑ Wang R, Xing X, Wang Y, Tran A, Crawford NM. A genetic screen for nitrate regulatory mutants captures the nitrate transporter gene NRT1.1. Plant Physiol. 2009 Sep;151(1):472-8. doi: 10.1104/pp.109.140434. Epub 2009 Jul, 24. PMID:19633234 doi:http://dx.doi.org/10.1104/pp.109.140434
↑ Krouk G, Lacombe B, Bielach A, Perrine-Walker F, Malinska K, Mounier E, Hoyerova K, Tillard P, Leon S, Ljung K, Zazimalova E, Benkova E, Nacry P, Gojon A. Nitrate-regulated auxin transport by NRT1.1 defines a mechanism for nutrient sensing in plants. Dev Cell. 2010 Jun 15;18(6):927-37. doi: 10.1016/j.devcel.2010.05.008. PMID:20627075 doi:http://dx.doi.org/10.1016/j.devcel.2010.05.008
↑ Parker JL, Newstead S. Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1. Nature. 2014 Mar 6;507(7490):68-72. doi: 10.1038/nature13116. Epub 2014 Feb 26. PMID:24572366 doi:http://dx.doi.org/10.1038/nature13116

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a2o"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the nitrate transporter NRT1.1 from Arabidopsis thaliana in complex with nitrate.==
 <StructureSection load='5a2o' size='340' side='right' caption='[[5a2o]], [[Resolution|resolution]] 3.71&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a2n|5a2n]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a2o RCSB], [http://www.ebi.ac.uk/pdbsum/5a2o PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2o OCA], [http://pdbe.org/5a2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a2o RCSB], [http://www.ebi.ac.uk/pdbsum/5a2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a2o ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5a2o" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

5a2o

From Proteopedia

Revision as of 17:07, 22 March 2017

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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