2zsh | pdb_00002zsh

Structural basis of gibberellin(GA3)-induced DELLA recognition by the gibberellin receptor

spinqualitylabelsall models 2zsh, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zsh is a 2 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 1.8Å Ligands: GA3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GID1A_ARATH Functions as soluble gibberellin (GA) receptor. GA is an essential hormone that regulates growth and development in plants. Binds with high affinity the biologically active gibberellin GA4, but has no affinity for the biologically inactive GAs. In response to GA, interacts with specific DELLA proteins, known as repressors of GA-induced growth, and targets them for degradation via proteasome. Seems to be required for GA signaling that controls root growth, seed germination, stem elongation and flower development. Partially redundant with GID1B and GID1C. Publication Abstract from PubMed Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors. Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.,Murase K, Hirano Y, Sun TP, Hakoshima T Nature. 2008 Nov 27;456(7221):459-63. PMID:19037309 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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