title: [NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101. II. Enzyme conformation at 3.0 A resolution].
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 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.
authors.forename: V S
authors.initials: VS
authors.lastname: Lamzin
authors.forename: A E
authors.initials: AE
authors.lastname: Aleshin
authors.forename: B O
authors.initials: BO
authors.lastname: Popov
authors.forename: E G
authors.initials: EG
authors.lastname: Arutiunian
mesh_terms: 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
chemical_list: D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases
vernacular_title: NAD-zavisimaia formiatdegidrogenaza metilotrofnykh bakteriĭ Pseudomonas sp. 101. II. Prostranstvennaia struktura fermenta pri razreshenii 3,0 A.