Figure 3

Comparison of the structures of hMOF and yEsa1. (A) Ribbon representation of hMOF acetyltransferase domain (hMOF PDB ID 2PQ8). Bound Coenzyme A is shown as a stick model, the atoms have standard colors. The Zn-finger domain of hMOF is colored blue, the central HAT domain green and the C-terminal domain is magenta. The amino acid side chains of the Zn-finger ligands (Cys 267, Cys 270, His 283, and Cys 287) are shown as a stick model. The Zn²⁺ atom is shown as a pink sphere. The side chains of active site residues Cys 373 (dMOF Cys 680; yEsa1 Cys 304) and Glu 407 (dMOF Glu 714; yESA1 Glu 338) mutated in dMOF in this study are also shown as ball and stick models, and the active site cleft is labeled. The position corresponding to Gly 691 (mof¹mutation in D. melanogaster MOF) (hMOF Gly 384; yESA1 Gly 315) is shown in orange and labeled. (B) Structural superposition of the HAT domains of hMOF (yellow-orange) and yESA1 (magenta) (Esa1 PDB ID 1FY7). Drawn as in (A) except that the position of Gly 384 of hMOF is shown in green and the Coenzyme A moiety is shown only for hMOF (Esa1 CoA omitted for clarity). Superposition carried out using lsqkab of the CCP4 package. Figures drawn with Molscript [54] and Raster3D [55].