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6l0v

From Proteopedia

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Current revision (10:45, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6l0v' size='340' side='right'caption='[[6l0v]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='6l0v' size='340' side='right'caption='[[6l0v]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6l0v]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L0V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6l0v]] is a 8 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=6L0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L0V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.347&#8491;</td></tr>
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<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=6l0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l0v OCA], [http://pdbe.org/6l0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l0v RCSB], [http://www.ebi.ac.uk/pdbsum/6l0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l0v ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l0v OCA], [https://pdbe.org/6l0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l0v RCSB], [https://www.ebi.ac.uk/pdbsum/6l0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l0v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F4K0X5_ARATH F4K0X5_ARATH]
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In many plant species, roots maintain specific growth angles relative to the direction of gravity, known as gravitropic set point angles (GSAs). These contribute to the efficient acquisition of water and nutrients. AtLAZY1/LAZY1-LIKE (LZY) genes are involved in GSA control by regulating auxin flow toward the direction of gravity in Arabidopsis. Here, we demonstrate that RCC1-like domain (RLD) proteins, identified as LZY interactors, are essential regulators of polar auxin transport. We show that interaction of the CCL domain of LZY with the BRX domain of RLD is important for the recruitment of RLD from the cytoplasm to the plasma membrane by LZY. A structural analysis reveals the mode of the interaction as an intermolecular beta-sheet in addition to the structure of the BRX domain. Our results offer a molecular framework in which gravity signal first emerges as polarized LZY3 localization in gravity-sensing cells, followed by polar RLD1 localization and PIN3 relocalization to modulate auxin flow.
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Polar recruitment of RLD by LAZY1-like protein during gravity signaling in root branch angle control.,Furutani M, Hirano Y, Nishimura T, Nakamura M, Taniguchi M, Suzuki K, Oshida R, Kondo C, Sun S, Kato K, Fukao Y, Hakoshima T, Morita MT Nat Commun. 2020 Jan 3;11(1):76. doi: 10.1038/s41467-019-13729-7. PMID:31900388<ref>PMID:31900388</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6l0v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Futrutani, M]]
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[[Category: Futrutani M]]
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[[Category: Hakoshima, T]]
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[[Category: Hakoshima T]]
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[[Category: Hirano, Y]]
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[[Category: Hirano Y]]
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[[Category: Morita, M T]]
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[[Category: Morita MT]]
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[[Category: Nishimura, T]]
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[[Category: Nishimura T]]
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[[Category: Taniguchi, M]]
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[[Category: Taniguchi M]]
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[[Category: Auxin]]
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[[Category: Brx domain]]
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[[Category: Gravitropic setpoint angle]]
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[[Category: Gravitropism]]
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[[Category: Signaling protein]]
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Current revision

Structure of RLD2 BRX domain bound to LZY3 CCL motif

PDB ID 6l0v

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