7qpc
From Proteopedia
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<StructureSection load='7qpc' size='340' side='right'caption='[[7qpc]], [[Resolution|resolution]] 3.44Å' scene=''> | <StructureSection load='7qpc' size='340' side='right'caption='[[7qpc]], [[Resolution|resolution]] 3.44Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[7qpc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qpc]] 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=7QPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.44Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLP:1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>DLP</scene>, <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=7qpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpc OCA], [https://pdbe.org/7qpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpc RCSB], [https://www.ebi.ac.uk/pdbsum/7qpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpc 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=7qpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpc OCA], [https://pdbe.org/7qpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpc RCSB], [https://www.ebi.ac.uk/pdbsum/7qpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PIN8_ARATH PIN8_ARATH] Component of the intracellular auxin-transport pathway in the male gametophyte (PubMed:20439545, PubMed:22540348). Involved in the regulation of auxin homeostasis in pollen (PubMed:22540348). Involved in the efflux of auxin from the endoplasmic reticulum into the cytoplasm (PubMed:22760640). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in the control of vein patterning (PubMed:23437008, PubMed:24304505). Redundantly with PIN6, inhibits the vein-formation-promoting functions of PIN5 (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462).<ref>PMID:20439545</ref> <ref>PMID:22540348</ref> <ref>PMID:22760640</ref> <ref>PMID:23437008</ref> <ref>PMID:24304505</ref> <ref>PMID:26560462</ref> <ref>PMID:22990451</ref> | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants(1-3). The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space(4-9). Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development. | Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants(1-3). The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space(4-9). Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development. | ||
| - | Structures and mechanism of the plant PIN-FORMED auxin transporter.,Ung KL, Winkler M, Schulz L, Kolb M, Janacek DP, Dedic E, Stokes DL, Hammes UZ, Pedersen BP Nature. 2022 | + | Structures and mechanism of the plant PIN-FORMED auxin transporter.,Ung KL, Winkler M, Schulz L, Kolb M, Janacek DP, Dedic E, Stokes DL, Hammes UZ, Pedersen BP Nature. 2022 Sep;609(7927):605-610. doi: 10.1038/s41586-022-04883-y. Epub 2022 , Jun 29. PMID:35768502<ref>PMID:35768502</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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dedic | + | [[Category: Dedic E]] |
| - | [[Category: Pedersen | + | [[Category: Pedersen BP]] |
| - | [[Category: Stokes | + | [[Category: Stokes DL]] |
| - | [[Category: Ung | + | [[Category: Ung KL]] |
| - | [[Category: Winkler | + | [[Category: Winkler MBL]] |
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Current revision
Inward-facing NPA bound form of auxin transporter PIN8
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