Fig. 7: Structures of S. venezuelae GlgX-c-di-GMP-acarbose complexes.
From: Allosteric regulation of glycogen breakdown by the second messenger cyclic di-GMP
a Structure of the S. venezuelae GlgX-c-di-GMP-acarbose complex (pH 8.5) (red) superimposed onto the S. venezuelae GlgX-c-di-GMP complex (cyan). The acarbose molecules are bound in the active site and shown as green spheres. The c-di-GMP molecules are bound at the ends, in the identical location in both structures. b Close up of the bound acarbose in the S. venezuelae GlgX-c-di-GMP-acarbose complex (red). Shown are the side chains of the residues that contact the acarbose in both the c-di-GMP-acarbose (red) and c-di-GMP bound (cyan) structures. c Structure of the S. venezuelae GlgX-c-di-GMP-acarbose complex solved at pH 4.5. In this structure, the acarbose has not reacted with GlgX (as density is evident for all sugar moieties). One GlgX subunit is cyan and the other red, the c-di-GMP and acarbose molecules are shown as sticks. The omit mFo-DFc map in which the ligands had been removed is also shown as a blue mesh and contoured at 4σ.
