Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase

A new crystallographic structure of the free active-site R conformer of the allosteric enzyme glucosamine-6-phosphate deaminase from Escherichia coli, coupled with previously reported structures of the T and R conformers, generates a detailed description of the heterotropic allosteric transition in which structural flexibility plays a central role.