Histone acetyltransferase

spinqualitylabelsall models Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry 1bob) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Histone acetyltransferase (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation. See also Histone acetyltransferase 1-2 Complex (HAT1/2). Histone acetyltransferase P300 acetylates all 4 core histones in nucleosomes and also non-histone targets. Relevance Inhibitors of HAT are potential drugs for inflammatory diseases. Disease Aberrant forms of HAT have been linked to congenital developmental disorders and various forms of cancer. Structural highlights HAT binds acetyl CoA in a cleft toward the center of the concave surface of the protein. Water molecules shown as red spheres. 3D Structures of histone acetyltransferase Histone acetyltransferase 3D structures

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