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EC Number
Crystallization
Reference
analysis of the electrostatic potentials of the interfaces between the subunits. Regions A, B, and C are almost electroneutral
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77
mutant enzymes R301K and R301A, hanging drop vapor diffusion method, using 0.1 M NaCl, 0.1 M sodium cacodylate pH 5.8, 16% PEG 6000 (w/v) (for mutant R301K) or 0.1 M ammonium acetate, 0.1 M Bis Tris pH 5.5, 17% PEG 10000 (w/v) (for mutant R301A)
Results 1 - 3 of 3