Fig. 1: H. pylori GR dimer structure bound to D-Glu (substrate) and Compound A (allosteric inhibitor).
From: Decrypting a cryptic allosteric pocket in H. pylori glutamate racemase
H. pylori GR exists as an obligate dimer, with the active sites of each monomer facing one another (D-Glu is shown in the center of each monomer in blue and red). Structure PDB 2JFZ (brown ribbons) bound to Compound A (shown in green) bound to the allosteric pocket is superposed onto the inhibitor free form of the enzyme PDB 2JFX (yellow ribbons). Mechanistically, these structures alone are not sufficient to understand allosteric inhibition in this system, which is largely driveni by dynamics, as discussed in the text.
