3T92

Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein

Summary for 3T92

• Entry DOI: 10.2210/pdb3t92/pdb
• Descriptor: HISTONE ACETYLTRANSFERASE P300 TAZ2-CCAAT/ENHANCER-BINDING PROTEIN EPSILON, ZINC ION, 3,3',3''-phosphanetriyltripropanoic acid, ... (6 entities in total)
• Functional Keywords: taz2 domain, zinc finger, transcription, 300/cbp, c/ebp proteins, transferase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 1
• Total formula weight: 14110.35

Authors

Bhaumik, P.,Maria, M. (deposition date: 2011-08-02, release date: 2012-08-08, Last modification date: 2024-02-28)

Primary citation

Bhaumik, P.,Davis, J.,Tropea, J.E.,Cherry, S.,Johnson, P.F.,Miller, M.
Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300.
Acta Crystallogr. D Biol. Crystallogr., 70:1914-1921, 2014

PubMed Abstract: Members of the C/EBP family of transcription factors bind to the Taz2 domain of p300/CBP and mediate its phosphorylation through the recruitment of specific kinases. Short sequence motifs termed homology boxes A and B, which comprise their minimal transactivation domains (TADs), are conserved between C/EBP activators and are necessary for specific p300/CBP binding. A possible mode of interaction between C/EBP TADs and the p300 Taz2 domain was implied by the crystal structure of a chimeric protein composed of residues 1723-1818 of p300 Taz2 and residues 37-61 of C/EBPℇ. The segment corresponding to the C/EBPℇ TAD forms two orthogonally disposed helices connected by a short linker and interacts with the core structure of Taz2 from a symmetry-related molecule. It is proposed that other members of the C/EBP family interact with the Taz2 domain in the same manner. The position of the C/EBPℇ peptide on the Taz2 protein interaction surface suggests that the N-termini of C/EBP proteins are unbound in the C/EBP-p300 Taz2 complex. This observation is in agreement with the known location of the docking site of protein kinase HIPK2 in the C/EBPβ N-terminus, which associates with the C/EBPβ-p300 complex.

PubMed: 25004968
DOI: 10.1107/S1399004714009262

Experimental method

X-RAY DIFFRACTION (1.5 Å)