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1t1h

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{{STRUCTURE_1t1h| PDB=1t1h | SCENE= }}
{{STRUCTURE_1t1h| PDB=1t1h | SCENE= }}
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'''NMR solution structure of the U box domain from AtPUB14, an armadillo repeat containing protein from Arabidopsis thaliana'''
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===NMR solution structure of the U box domain from AtPUB14, an armadillo repeat containing protein from Arabidopsis thaliana===
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==Overview==
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U-box proteins, as well as other proteins involved in regulated protein degradation, are apparently over-represented in Arabidopsis compared with other model eukaryotes. The Arabidopsis protein AtPUB14 contains a typical U-box domain followed by an Armadillo repeat region, a domain organization that is frequently found in plant U-box proteins. In vitro ubiquitination assays demonstrated that AtPUB14 functions as an E3 ubiquitin ligase with specific E2 ubiquitin-conjugating enzymes. The structure of the AtPUB14 U-box domain was determined by NMR spectroscopy. It adopts the betabetaalphabeta fold of the Prp19p U-box and RING finger domains. In these proteins, conserved hydrophobic residues form a putative E2-binding cleft. By contrast, they contain no common polar E2 binding site motif. Two hydrophobic cores stabilize the AtPUB14 U-box fold, and hydrogen bonds and salt bridges interconnect the residues corresponding to zinc ion-coordinating residues in RING domains. Residues from a C-terminal alpha-helix interact with the core domain and contribute to stabilization. The Prp19p U-box lacks a corresponding C-terminal alpha-helix. Chemical shift analysis suggested that aromatic residues exposed at the N terminus and the C-terminal alpha-helix of the AtPUB14 U-box participate in dimerization. Thus, AtPUB14 may form a biologically relevant dimer. This is the first plant U-box structure to be determined, and it provides a model for studies of the many plant U-box proteins and their interactions. Structural insight into these interactions is important, because ubiquitin-dependent protein degradation is a prevalent regulatory mechanism in plants.
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(as it appears on PubMed at http://www.pubmed.gov), where 15231834 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15231834}}
==About this Structure==
==About this Structure==
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1T1H is a [[Single protein]] structure of sequence 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=1T1H OCA].
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1T1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1H OCA].
==Reference==
==Reference==
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[[Category: U-box]]
[[Category: U-box]]
[[Category: Ubiquitin ligase]]
[[Category: Ubiquitin ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:45:23 2008''

Revision as of 14:45, 28 July 2008

Image:1t1h.png

Template:STRUCTURE 1t1h

NMR solution structure of the U box domain from AtPUB14, an armadillo repeat containing protein from Arabidopsis thaliana

Template:ABSTRACT PUBMED 15231834

About this Structure

1T1H is a Single protein structure of sequence from Arabidopsis thaliana. Full experimental information is available from OCA.

Reference

Structure and biochemical function of a prototypical Arabidopsis U-box domain., Andersen P, Kragelund BB, Olsen AN, Larsen FH, Chua NH, Poulsen FM, Skriver K, J Biol Chem. 2004 Sep 17;279(38):40053-61. Epub 2004 Jun 30. PMID:15231834

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