3P57
Crystal structure of the p300 TAZ2 domain bound to MEF2 on DNA
Summary for 3P57
Entry DOI | 10.2210/pdb3p57/pdb |
Descriptor | Myocyte-specific enhancer factor 2A, DNA (5'-D(*A*AP*AP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*GP*A)-3'), DNA (5'-D(*TP*TP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*TP*T)-3'), ... (6 entities in total) |
Functional Keywords | protein-dna complex, transcription factor, transcriptional activation, p300, zinc finger, transferase-transcription activator-dna complex, transferase/transcription activator/dna |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 13 |
Total formula weight | 104442.81 |
Authors | He, J.,Ye, J.,Riquelme, C.,Liu, J.O. (deposition date: 2010-10-08, release date: 2011-08-10, Last modification date: 2023-09-06) |
Primary citation | He, J.,Ye, J.,Cai, Y.,Riquelme, C.,Liu, J.O.,Liu, X.,Han, A.,Chen, L. Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly. Nucleic Acids Res., 39:4464-4474, 2011 Cited by PubMed Abstract: Transcription co-activators CBP and p300 are recruited by sequence-specific transcription factors to specific genomic loci to control gene expression. A highly conserved domain in CBP/p300, the TAZ2 domain, mediates direct interaction with a variety of transcription factors including the myocyte enhancer factor 2 (MEF2). Here we report the crystal structure of a ternary complex of the p300 TAZ2 domain bound to MEF2 on DNA at 2.2Å resolution. The structure reveals three MEF2:DNA complexes binding to different sites of the TAZ2 domain. Using structure-guided mutations and a mammalian two-hybrid assay, we show that all three interfaces contribute to the binding of MEF2 to p300, suggesting that p300 may use one of the three interfaces to interact with MEF2 in different cellular contexts and that one p300 can bind three MEF2:DNA complexes simultaneously. These studies, together with previously characterized TAZ2 complexes bound to different transcription factors, demonstrate the potency and versatility of TAZ2 in protein-protein interactions. Our results also support a model wherein p300 promotes the assembly of a higher-order enhanceosome by simultaneous interactions with multiple DNA-bound transcription factors. PubMed: 21278418DOI: 10.1093/nar/gkr030 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1921 Å) |
Structure validation
Download full validation report