2GS0

NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the activation domain of p53

Summary for 2GS0

• Entry DOI: 10.2210/pdb2gs0/pdb
• NMR Information: BMRB: 6225
• Descriptor: RNA polymerase II transcription factor B subunit 1, Cellular tumor antigen p53 (2 entities in total)
• Functional Keywords: p53, tfiih, tfb1, activation, transcription, ph domain
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P32776; Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 2
• Total formula weight: 18922.37

Authors

Di Lello, P.,Jones, T.N.,Nguyen, B.D.,Legault, P.,Omichinski, J.G. (deposition date: 2006-04-25, release date: 2006-10-31, Last modification date: 2024-05-29)

Primary citation

Di Lello, P.,Jenkins, L.M.,Jones, T.N.,Nguyen, B.D.,Hara, T.,Yamaguchi, H.,Dikeakos, J.D.,Appella, E.,Legault, P.,Omichinski, J.G.
Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53.
Mol.Cell, 22:731-740, 2006

PubMed Abstract: The interaction between the amino-terminal transactivation domain (TAD) of p53 and TFIIH is directly correlated with the ability of p53 to activate both transcription initiation and elongation. We have identified a region within the p53 TAD that specifically interacts with the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH. We have solved the 3D structure of a complex between the p53 TAD and the PH domain of Tfb1 by NMR spectroscopy. Our structure reveals that p53 forms a nine residue amphipathic alpha helix (residues 47-55) upon binding to Tfb1. In addition, we demonstrate that diphosphorylation of p53 at Ser46 and Thr55 leads to a significant enhancement in p53 binding to p62 and Tfb1. These results indicate that a phosphorylation cascade involving Ser46 and Thr55 of p53 could play an important role in the regulation of select p53 target genes.

PubMed: 16793543
DOI: 10.1016/j.molcel.2006.05.007

Experimental method

SOLUTION NMR