Fig. 5: Structure of LDTGo.
A Overview of the LDTGo structure, colored from the N-terminus (blue) to the C-terminus (red). B Superimposition of LDTGo (green) and the catalytic domain of YcbBEc (blue) bound to meropenem (yellow). Three characteristic features are highlighted, i) the capping loop of both enzymes, which in LDTGo is disordered, ii) the LDTGo catalytic residues C264 and H245, and iii) the distinctive LDTGo domain within the active site composed of 2 interconnected loops between the β-strands 3 and 4 (Lβ3-β4) and the β-strands 5 and 6 and (Lβ5-β6). C Surface representation of LDT Go (green) with the Pro-rich belt shown as sticks (C-atoms colored in purple). The catalytic Cys is shown in yellow. Zoom-in panels show the hydrogen bonds formed between the belt and the rest of the protein. D Superimposition of the LDTGo structure (green) and its Alphafold2 prediction model (light brown), with the main differences highlighted in the zoom-in panels.
