3IO2

Crystal structure of the Taz2 domain of p300

3IO2 の概要

• エントリーDOI: 10.2210/pdb3io2/pdb
• 関連するPDBエントリー: 2K8F
• 分子名称: Histone acetyltransferase p300, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: p300, metal-binding, transcription, zinc-finger, bromodomain, cell cycle, citrullination, disease mutation, host-virus interaction, methylation, nucleus, phosphoprotein, transcription regulation, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q09472
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13568.86

構造登録者

Miller, M.,Dauter, Z.,Wlodawer, A. (登録日: 2009-08-13, 公開日: 2009-11-24, 最終更新日: 2024-02-21)

主引用文献

Miller, M.,Dauter, Z.,Cherry, S.,Tropea, J.E.,Wlodawer, A.
Structure of the Taz2 domain of p300: insights into ligand binding.
Acta Crystallogr.,Sect.D, 65:1301-1308, 2009

PubMed Abstract: CBP and its paralog p300 are histone acetyl transferases that regulate gene expression by interacting with multiple transcription factors via specialized domains. The structure of a segment of human p300 protein (residues 1723-1836) corresponding to the extended zinc-binding Taz2 domain has been investigated. The crystal structure was solved by the SAD approach utilizing the anomalous diffraction signal of the bound Zn ions. The structure comprises an atypical helical bundle stabilized by three Zn ions and closely resembles the solution structures determined previously for shorter peptides. Residues 1813-1834 from the current construct form a helical extension of the C-terminal helix and make extensive crystal-contact interactions with the peptide-binding site of Taz2, providing additional insights into the mechanism of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and molecular modeling, a hypothetical model of the binding of phosphorylated p53 TAD1 to Taz2 has been proposed.

PubMed: 19966416
DOI: 10.1107/S0907444909040153

実験手法

X-RAY DIFFRACTION (2.5 Å)