2p1o
From Proteopedia
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | SKP1A, ASK1, SKP1, UIP1 (Arabidopsis thaliana), TIR1, FBL1, WEI1 (Arabidopsis thaliana) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mechanism of Auxin Perception by the TIR1 ubiquitin ligase
Overview
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.
About this Structure
2P1O is a Protein complex structure of sequences from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
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
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