Figure 3: The structure of PA3825EAL in complex with c-di-GMP/Mg2+. | Scientific Reports

Figure 3: The structure of PA3825EAL in complex with c-di-GMP/Mg2+.

From: Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases

Figure 3

C-di-GMP is shown as yellow sticks and Mg2+ ions are represented by magenta spheres. Zoomed views of the β5-α5 loop, highlighted in light-blue, demonstrate the variation in the length of the α5 helix between the apo form and substrate forms of PA3825EAL. The structural shift in the β5-α5 loop allows Asp160 and Asp 161 to coordinate catalytic metals indicated as M1 and M2.

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