Fig. 6: c-di-GMP induces long-range conformational changes in S. venezuelae GlgX impacting the active site.
From: Allosteric regulation of glycogen breakdown by the second messenger cyclic di-GMP
Shown is an overlay of similar Cα atoms of apo GlgX (tan) onto the GlgX-c-di-GMP structure (cyan). The c-di-GMP bound in the GlgX-c-di-GMP structure is also colored cyan. Structural changes upon c-di-GMP binding occur in the C-terminal c-di-GMP binding region with residues 579–593 and 432–442 shifting in position. These structural changes lead to reorganization of residues 377-396 and residues 341–355, both of which contain key catalytic residues. The regions that undergo conformational changes are colored blue for the c-di-GMP bound state and yellow for the apo state. This is how c-di-GMP, which binds 30 Å from the active site, can induce changes that result in reorganization of the active site.
