Figure 1 | Scientific Reports

Figure 1

From: X-Ray snapshots of a pyridoxal enzyme: a catalytic mechanism involving concerted [1,5]-hydrogen sigmatropy in methionine γ-lyase

Figure 1

Structure of substrate-free EhMGL1. (a) Cartoon representation of the EhMGL1 homotetramer structure. A, B, C and D chains are colored in teal, deep green, yellow and pink, respectively. Two catalytic dimers are formed by A–D and B–C pairs. PLP-enzyme (Lys205) imine bound to each chain is shown as spheres with the color code C (white), N (blue), O (red) and P (orange). (b) Structure of the A chain. The N-terminal, PLP-binding and C-terminal domains are colored in light orange, teal and purple, respectively. The bound PLP-enzyme (Lys205) imine is shown as in (a). The α2*/α3* loop from the D chain is represented as a pink cartoon and contributes to the formation of the active site of the A chain. (c) Stick representation of the active site of the A chain. The color code of PLP-enzyme (Lys205) imine is the same as in (a). Residues from the PLP-binding domain are colored in teal, and residues from the α2*/α3* loop of the D chain are colored in pink. Dashed lines indicate hydrogen bonds. Numbering of the nitrogen and carbon atoms of PLP is shown in the inset. The images were generated using PyMOL 39.

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