[NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101. II. Enzyme conformation at 3.0 A resolution].
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 C alpha-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.
Lamzin
V S
VS
Aleshin
A E
AE
Popov
B O
BO
Arutiunian
E G
EG
D000445:Aldehyde Oxidoreductases / Q000032:analysis*; D001665:Binding Sites; D005560:Formate Dehydrogenases / Q000032:analysis*; D008958:Models, Molecular; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D013045:Species Specificity; D014961:X-Ray Diffraction
D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases
NAD-zavisimaia formiatdegidrogenaza metilotrofnykh bakteriĭ Pseudomonas sp. 101. II. Prostranstvennaia struktura fermenta pri razreshenii 3,0 A.