Structure Analysis of Entamoeba histolytica DNMT2 (EhMeth)
Figure 1
The crystal structure of EhMeth.
(A) Secondary structure representation: α-helices are shown in blue, β-strands in red while loop regions are depicted in grey. Clearly the active site helix is protruding from the large domain. (B) The main-chain of EhMeth is shown in relation to its B-factor. Increased B-factors indicate a higher flexibility of the respective area of the structure, which can be observed in the active site helix and some loop areas in the small domain. (C) Surface charge representation: the proximal side of EhMeth is predominantly positively charged (blue), while the distal side of EhMeth mainly displays neutral and negative surface charges (grey, red). On the positively charged surface – the putative DNA/RNA binding area – also the cofactor-binding pocket can be seen (AdoHcy is shown in green). A dashed circle highlights a highly negatively charged pocket on the distal side of EhMeth.