2p1o
From Proteopedia
| Line 20: | Line 20: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2P1O is a | + | 2P1O is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1O OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:17410169</ref><references group="xtra"/> | |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Calderon-Villalobos, L I.A.]] | [[Category: Calderon-Villalobos, L I.A.]] | ||
[[Category: Estelle, M.]] | [[Category: Estelle, M.]] | ||
| Line 35: | Line 34: | ||
[[Category: Leucine rich repeat]] | [[Category: Leucine rich repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:20:28 2009'' |
Revision as of 14:20, 16 February 2009
Mechanism of Auxin Perception by the TIR1 ubiquitin ligase
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.
About this Structure
2P1O is a 3 chains structure of sequences from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
- Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N. Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature. 2007 Apr 5;446(7136):640-5. PMID:17410169 doi:10.1038/nature05731
Page seeded by OCA on Mon Feb 16 16:20:28 2009
