title: Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity.
abstract: Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only enzyme from Archaea among the structurally studied members of the medium-chain ADH family described so far. Here, we present the three-dimensional structure of the apo form of the mutant N249Y which exhibits increased catalytic activity when compared to the wild-type enzyme. The substitution, located in the coenzyme binding domain, decreases the affinity for NAD(H) cofactor. The rearrangement of segments 248-250 and 270-275, induced by the mutation, suggests an explanation for the lower coenzyme affinity. This study also highlights the role in SsADH catalysis of the flexible loops located at the interface between the catalytic and the coenzyme domains.
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6-8, I-80134 Naples, Italy.
authors.forename: Luciana
authors.initials: L
authors.lastname: Esposito
authors.forename: Ilaria
authors.initials: I
authors.lastname: Bruno
authors.forename: Filomena
authors.initials: F
authors.lastname: Sica
authors.forename: Carlo Antonio
authors.initials: CA
authors.lastname: Raia
authors.forename: Antonietta
authors.initials: A
authors.lastname: Giordano
authors.forename: Mosè
authors.initials: M
authors.lastname: Rossi
authors.forename: Lelio
authors.initials: L
authors.lastname: Mazzarella
authors.forename: Adriana
authors.initials: A
authors.lastname: Zagari
mesh_terms: D000426:Alcohol Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D003067:Coenzymes / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D017354:Point Mutation; D011487:Protein Conformation; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics
chemical_list: D003067:Coenzymes; D000426:Alcohol Dehydrogenase