2p1m: Difference between revisions
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'''TIR1-ASK1 complex structure''' | {{Structure | ||
|PDB= 2p1m |SIZE=350|CAPTION= <scene name='initialview01'>2p1m</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=IHP:INOSITOL HEXAKISPHOSPHATE'>IHP</scene> | |||
|ACTIVITY= | |||
|GENE= SKP1A, ASK1, SKP1, UIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), TIR1, FBL1, WEI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |||
}} | |||
'''TIR1-ASK1 complex structure''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2P1M is a [ | 2P1M is a [[Protein complex]] 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=2P1M OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17410169 17410169] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: leucine rich repeat]] | [[Category: leucine rich repeat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:07:22 2008'' | ||
Revision as of 16:07, 20 March 2008
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| 2p1m, resolution 1.80Å | |||||||||||||
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| Ligands: | IHP | ||||||||||||
| Gene: | SKP1A, ASK1, SKP1, UIP1 (Arabidopsis thaliana), TIR1, FBL1, WEI1 (Arabidopsis thaliana) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
TIR1-ASK1 complex structure
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
2P1M 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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