NAD-DEPENDENT FORMATE DEHYDROGENASE FROM METHYLOTROPHIC BACTERIUM PSEUDOMONAS sp. 101. II. THREE-DIMENSIONAL STRUCTURE AT 3.0 A RESOLUTION
V. S. LAMZIN, A. E. ALESHIN*. V. O. POPOV, E. H. HARUTYUNYAN
A. N, Bach Institute of Biochemistry, Academy of Sciences of the USSR, Moscow; * A. V. Shubnikov Institute of Crystallography, Academy of Sciences of the USSR, Moscow
Abstract: Three heavy atom isomorphous derivatives were used for the X-ray analysis of the holo form of NAD-dependent bacterial formate dehydrogenase (ternary complex enzyme-NAD-azide) at 3.0 A resolution. The enzyme subunit contains a catalytic and a coenzyme binding domain, with the active centre and the coenzyme binding site in the cleft between the domains. The polypeptide chain's fold and the position of 393 Cα-atoms were determined. The secondary structure of the formate dehydrogenase was resolved. The structure of the NAD-binding domain is shown to be similar to that of other NAD-dependent enzymes.
Russian Journal of Bioorganic Chemistry 1990, 16 (3):336-344