6l0w

Structure of RLD2 BRX domain bound to LZY3 CCL motif

spinqualitylabelsall models 6l0w, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l0w is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.591Å Ligands: EDO, FLC, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F4K0X5_ARATH Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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