3EXJ

Crystal Structure of a p53 Core Tetramer Bound to DNA

Summary for 3EXJ

• Entry DOI: 10.2210/pdb3exj/pdb
• Related: 3EXL
• Descriptor: mouse p53 core domain, 5'-D(P*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DCP*DA)-3', 5'-D(*DTP*DTP*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DC)-3', ... (6 entities in total)
• Functional Keywords: protein-dna complex, acetylation, activator, anti-oncogene, apoptosis, cell cycle, covalent protein-rna linkage, cytoplasm, disease mutation, dna-binding, endoplasmic reticulum, metal-binding, methylation, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation, zinc, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm : P02340
• Total number of polymer chains: 4
• Total formula weight: 52098.64

Authors

Malecka, K.A. (deposition date: 2008-10-16, release date: 2008-12-16, Last modification date: 2023-12-27)

Primary citation

Malecka, K.A.,Ho, W.C.,Marmorstein, R.
Crystal structure of a p53 core tetramer bound to DNA.
Oncogene, 28:325-333, 2009

PubMed Abstract: The tumor suppressor p53 regulates downstream genes in response to many cellular stresses and is frequently mutated in human cancers. Here, we report the use of a crosslinking strategy to trap a tetrameric p53 DNA-binding domain (p53DBD) bound to DNA and the X-ray crystal structure of the protein/DNA complex. The structure reveals that two p53DBD dimers bind to B form DNA with no relative twist and that a p53 tetramer can bind to DNA without introducing significant DNA bending. The numerous dimer-dimer interactions involve several strictly conserved residues, thus suggesting a molecular basis for p53DBD-DNA binding cooperativity. Surface residue conservation of the p53DBD tetramer bound to DNA highlights possible regions of other p53 domain or p53 cofactor interactions.

PubMed: 18978813
DOI: 10.1038/onc.2008.400

Experimental method

X-RAY DIFFRACTION (2 Å)