To date, an experimentally determined structure is only available for one PEtN transferase, the chromosomally encoded EptA enzyme from N. meningitidis . On the basis of this structure, these authors undertook a series of molecular dynamics (MD) simulations of EptA within the membrane environment, and in two of six 100 ns trajectories observed the enzyme to undergo a significant conformational change in which the catalytic domain underwent a rotation about the loop connecting the two domains, relative to the transmembrane domain and the membrane, allowing for new membrane contacts and even deformation of the membrane surface. It was hypothesized that this flexibility could allow for entry to the active site of two substrates of differing sizes, and so may be important to reactivity of the enzyme. Biophysical studies , primarily using small-angle X-ray scattering (SAXS), were considered to support this contention by identifying differences in the conformation of N. meningtidis EptA in micelles of two different detergents, n-dodecyl-β-d-maltoside (DDM) and n-dodecyl-phosphocholine (DPC), with the latter promoting a more open, extended organization. To date, however, no such investigations have been reported for any MCR enzyme.