7wkw
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7wkw]] 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=7WKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WKW FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wkw]] 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=7WKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WKW FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E7O:2-(naphthalen-1-ylcarbamoyl)benzoic+acid'>E7O</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.62Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E7O:2-(naphthalen-1-ylcarbamoyl)benzoic+acid'>E7O</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=7wkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wkw OCA], [https://pdbe.org/7wkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wkw RCSB], [https://www.ebi.ac.uk/pdbsum/7wkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wkw ProSAT]</span></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=7wkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wkw OCA], [https://pdbe.org/7wkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wkw RCSB], [https://www.ebi.ac.uk/pdbsum/7wkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wkw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PIN3_ARATH PIN3_ARATH] Acts as a component of the auxin efflux carrier. Seems to be involved in the lateral auxin transport system and mediates tropic growth. Coordinated polar localization of PIN3 is directly regulated by the vesicle trafficking process.<ref>PMID:20439545</ref> | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The PIN-FORMED (PIN) protein family of auxin transporters mediates polar auxin transport and has crucial roles in plant growth and development(1,2). Here we present cryo-electron microscopy structures of PIN3 from Arabidopsis thaliana in the apo state and in complex with its substrate indole-3-acetic acid and the inhibitor N-1-naphthylphthalamic acid (NPA). A. thaliana PIN3 exists as a homodimer, and its transmembrane helices 1, 2 and 7 in the scaffold domain are involved in dimerization. The dimeric PIN3 forms a large, joint extracellular-facing cavity at the dimer interface while each subunit adopts an inward-facing conformation. The structural and functional analyses, along with computational studies, reveal the structural basis for the recognition of indole-3-acetic acid and NPA and elucidate the molecular mechanism of NPA inhibition on PIN-mediated auxin transport. The PIN3 structures support an elevator-like model for the transport of auxin, whereby the transport domains undergo up-down rigid-body motions and the dimerized scaffold domains remain static. | The PIN-FORMED (PIN) protein family of auxin transporters mediates polar auxin transport and has crucial roles in plant growth and development(1,2). Here we present cryo-electron microscopy structures of PIN3 from Arabidopsis thaliana in the apo state and in complex with its substrate indole-3-acetic acid and the inhibitor N-1-naphthylphthalamic acid (NPA). A. thaliana PIN3 exists as a homodimer, and its transmembrane helices 1, 2 and 7 in the scaffold domain are involved in dimerization. The dimeric PIN3 forms a large, joint extracellular-facing cavity at the dimer interface while each subunit adopts an inward-facing conformation. The structural and functional analyses, along with computational studies, reveal the structural basis for the recognition of indole-3-acetic acid and NPA and elucidate the molecular mechanism of NPA inhibition on PIN-mediated auxin transport. The PIN3 structures support an elevator-like model for the transport of auxin, whereby the transport domains undergo up-down rigid-body motions and the dimerized scaffold domains remain static. | ||
| - | Structures and mechanisms of the Arabidopsis auxin transporter PIN3.,Su N, Zhu A, Tao X, Ding ZJ, Chang S, Ye F, Zhang Y, Zhao C, Chen Q, Wang J, Zhou CY, Guo Y, Jiao S, Zhang S, Wen H, Ma L, Ye S, Zheng SJ, Yang F, Wu S, Guo J Nature. 2022 Sep;609(7927):616-621. doi: 10.1038/s41586-022-05142-w. Epub 2022, Aug 2. PMID:35917926<ref>PMID:35917926</ref> | + | Structures and mechanisms of the Arabidopsis auxin transporter PIN3.,Su N, Zhu A, Tao X, Ding ZJ, Chang S, Ye F, Zhang Y, Zhao C, Chen Q, Wang J, Zhou CY, Guo Y, Jiao S, Zhang S, Wen H, Ma L, Ye S, Zheng SJ, Yang F, Wu S, Guo J Nature. 2022 Sep;609(7927):616-621. doi: 10.1038/s41586-022-05142-w. Epub 2022 , Aug 2. PMID:35917926<ref>PMID:35917926</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
NPA bound state of AtPIN3
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