2p1q
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
[[2p1q]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. The February 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Auxin and TIR1 Ubiquitin Ligase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_2 10.2210/rcsb_pdb/mom_2009_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1Q OCA]. | [[2p1q]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. The February 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Auxin and TIR1 Ubiquitin Ligase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_2 10.2210/rcsb_pdb/mom_2009_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1Q OCA]. | ||
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| + | ==See Also== | ||
| + | *[[Herbicide 2%2C4-D bound to TIR1 Ubiquitin Ligase|Herbicide 2%2C4-D bound to TIR1 Ubiquitin Ligase]] | ||
| + | *[[TIR1 ubiquitin ligase|TIR1 ubiquitin ligase]] | ||
==Reference== | ==Reference== | ||
Revision as of 07:21, 13 June 2012
Contents |
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
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.
See Also
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
