1T1H
NMR solution structure of the U box domain from AtPUB14, an armadillo repeat containing protein from Arabidopsis thaliana
Summary for 1T1H
| Entry DOI | 10.2210/pdb1t1h/pdb |
| Related | 1N87 |
| NMR Information | BMRB: 6265 |
| Descriptor | armadillo repeat containing protein (1 entity in total) |
| Functional Keywords | ubiquitin ligase, e3 ligase, arabidopsis, u-box, ligase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 8762.99 |
| Authors | Andersen, P.,Kragelund, B.B.,Olsen, A.N.,Larsen, F.H.,Chua, N.-H.,Poulsen, F.M.,Skriver, K. (deposition date: 2004-04-16, release date: 2004-08-03, Last modification date: 2024-05-22) |
| Primary citation | Andersen, P.,Kragelund, B.B.,Olsen, A.N.,Larsen, F.H.,Chua, N.-H.,Poulsen, F.M.,Skriver, K. Structure and Biochemical Function of a Prototypical Arabidopsis U-box Domain J.Biol.Chem., 279:40053-40061, 2004 Cited by PubMed Abstract: 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. PubMed: 15231834DOI: 10.1074/jbc.M405057200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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