| 1AIE |
P53 Tetramerization |
date |
Apr 17, 1997 |
|---|
| title | P53 Tetramerization Domain Crystal Structure |
| authors | P.R.E.Mittl, P.Chene, M.G.Gruetter |
| compound |
source |
Molecule: P53
Chain: Null
Fragment: Tetramerization Domain
Engineered: Yes
Biological_unit: Active As A Tetramer
|
Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
Expression_system_strain: Bl21
Expression_system_vector_type: Pgex-2t
|
| symmetry | Space Group: P 4 2 2
| R_factor | 0.191 |
crystal
cell |
| length a |
length b |
length c |
angle alpha |
angle beta |
angle gamma |
| 45.500 |
45.500 |
33.200 |
90.00 |
90.00 |
90.00 |
|
| method | X-Ray Diffraction | resolution | 1.5 Å |
| note | 1AIE is a representative structure |
| related structures | by homologous chain: 1C26 |
| domain | The nuclear export signal acts as a transcriptional repression domain. |
| similarity | Belongs to the P53 family. |
| subunit | This complex formation requires an additional factor, e6-ap, which stably associates with tp53 in the presence of e6. Binds dna as a homotetramer. In vitro, the interaction of tp53 with cancer-associated/hpv (e6) viral proteins leads to ubiquitination and degradation of tp53 giving a possible model for cell growth regulation. C-terminus interacts with taf1, when taf1 is part of the tfiid complex. |
| post-translat. modifications | O-linked glycosylation in the c-terminal basic region was studied in eb-1 cell line. Acetylated. Phosphorylated on thr-55 by taf1 which promotes mdm2-mediated degradation. Phosphorylation on ser residues mediates transcriptional activation. Deacetylation of lys-382 by sirt1 impairs its ability to induce proapoptotic program and modulate cell senescence. Phosphorylated on thr-18 by vrk1, which may prevent the interaction with mdm2. Sv40 small t antigen inhibits the dephosphorylation by the ac form of pp2a. Dephosphorylated by pp2a. |
| subcellular loc. | Cytoplasmic and nuclear. |
| Primary reference | Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template., Mittl PR, Chene P, Grutter MG, Acta Crystallogr D Biol Crystallogr 1998 Jan 1;54 ( Pt 1):86-9. PMID:9761820 |
: 