Secondary structure of the MutT enzyme as determined by NMR

The backbone NMR assignments for H-alpha, C-alpha, HN, N and carbonyl C' resonances based on 2D and 3D homonuclear and heteronuclear NMR spectra and amide NH exchange data were used to establish the secondary structure of MutT in solution. A pair of alpha-helices, spanning residues 47-59 and 119-128, are evident in MuT. MuT's nine proline residues are trans.