Solution Structure of Dimeric SAM Domain from MAPKKK Ste11
Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex.
Structure has been determined by 3-D NMR
Total distant constraints used, 1, 140, inter-subnuint NOE: 40, intra-subunit NOE:1134, dihedral angle:60
0.8 mM Ste11 SAM, U-15N, 13C, 10mM phosphate buffer, 300 mM NaCl, 90% H2O, 10% D2O
0.8mM Ste11 SAM U-15N, 13C mixed with unlabelled Ste11 SAM, 90% H2O, 10% D2O
SAM domain, MAP kinase, Ste11, TRANSFERASE