2p1q | pdb_00002p1q

Mechanism of Auxin Perception by the TIR1 ubiquitin ligase

spinqualitylabelsall models 2p1q, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2p1q is a 3 chain structure with sequence from Arabidopsis thaliana. The February 2009 RCSB PDB Molecule of the Month feature on Auxin and TIR1 Ubiquitin Ligase by David Goodsell is 10.2210/rcsb_pdb/mom_2009_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IAC, IHP Related: 2p1m, 2p1n, 2p1o, 2p1p Gene: SKP1A, ASK1, SKP1, UIP1 (Arabidopsis thaliana), TIR1, FBL1, WEI1 (Arabidopsis thaliana) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Auxin is a pivotal plant hormone that controls many aspects of plant growth and development. Perceived by a small family of F-box proteins including transport inhibitor response 1 (TIR1), auxin regulates gene expression by promoting SCF ubiquitin-ligase-catalysed degradation of the Aux/IAA transcription repressors, but how the TIR1 F-box protein senses and becomes activated by auxin remains unclear. Here we present the crystal structures of the Arabidopsis TIR1-ASK1 complex, free and in complexes with three different auxin compounds and an Aux/IAA substrate peptide. These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket. Anchored to the base of the TIR1 pocket, auxin binds to a partially promiscuous site, which can also accommodate various auxin analogues. Docked on top of auxin, the Aux/IAA substrate peptide occupies the rest of the TIR1 pocket and completely encloses the hormone-binding site. By filling in a hydrophobic cavity at the protein interface, auxin enhances the TIR1-substrate interactions by acting as a 'molecular glue'. Our results establish the first structural model of a plant hormone receptor. Mechanism of auxin perception by the TIR1 ubiquitin ligase.,Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N Nature. 2007 Apr 5;446(7136):640-5. PMID:17410169 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TIR1 ubiquitin ligase Transport inhibitor response 1 Ubiquitin protein ligase

Proteopedia Page Contributors and Editors (what is this?)

OCA