Figure 1
From: Alternative catalytic residues in the active site of Esco acetyltransferases
Structure of the MmEsco2368–592/CoA complex. (A) Sequence alignment49 of Esco orthologs. Sequences shown are Mus musculus MmEsco1, MmEsco2, Homo sapiens HsESCO1, HsESCO2, Xenopus laevis XlEco2 and S. cerevisiae ScEco1. Invariant residues are shown with a red background, and highly conserved residues are boxed. Numbering and secondary structural elements above the sequence alignment are for the MmEsco2368–592 sequence. Dashed lines mark the disordered regions. Blue circles indicate residues that might be involved in the abstraction of the proton from the ε-amino group of the substrate lysine. (B) Ribbon representation of the MmEsco2368–592/CoA complex. α-helices are shown in blue, β-strands in raspberry, and loop regions in grey. CoA is represented as sticks and colored according to elements: carbon, green; nitrogen, blue; sulfur, orange; oxygen, red and the zinc ion shown as a magenta sphere. There is an unresolved region in a loop connecting β6 and β7. Start and end point of this region is indicated by empty circles. (C) Numbering of equivalent putative catalytic residues of MmEsco2 in MmEsco1 and HsESCO1 sequences. Figure adapted from50.
