Figure 5
From: Ligand-driven conformational changes of MurD visualized by paramagnetic NMR
Summary of conformational changes of MurD that modulate the affinities for the ligands.
Apo MurD, with domain 3 existing in open state, has high affinity for ATP-Mg2+ but has low affinity for UMA or d-Glu. Binding of ATP-Mg2+ triggers conformational change of MurD to semi-closed conformation where the domain 3 is located in between open and closed state. Semi-closed state has higher affinity for UMA, but still has low affinity for d-Glu. Binding of UMA doesn’t change the conformation, but hydrolysis of ATP into ADP allows MurD to fully closed conformation that has higher affinity for d-Glu.
