title: Crystal structure of a putative CN hydrolase from yeast.
abstract: The crystal structure of a yeast hypothetical protein with sequence similarity to CN hydrolases has been determined to 2.4 A resolution by the multiwavelength anomalous dispersion (MAD) method. The protein folds as a four-layer alphabetabetaalpha sandwich and exists as a dimer in the crystal and in solution. It was selected in a structural genomics project as representative of CN hydrolases at a time when no structures had been determined for members of this family. Structures for two other members of the family have since been reported and the three proteins have similar topology and dimerization modes, which are distinct from those of other alphabetabetaalpha proteins whose structures are known. The dimers form an unusual eight-layer alphabetabetaalpha:alphabetabetaalpha structure. Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. As with serine hydrolases, the active-site nucleophile (cysteine in this case) is positioned on a nucleophile elbow.
authors.affiliation: Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.
authors.forename: Desigan
authors.initials: D
authors.lastname: Kumaran
authors.forename: Subramaniam
authors.initials: S
authors.lastname: Eswaramoorthy
authors.forename: Sue Ellen
authors.initials: SE
authors.lastname: Gerchman
authors.forename: Helen
authors.initials: H
authors.lastname: Kycia
authors.forename: F William
authors.initials: FW
authors.lastname: Studier
authors.forename: Subramanyam
authors.initials: S
authors.lastname: Swaminathan
mesh_terms: D017766:Acid Anhydride Hydrolases; D000581:Amidohydrolases / Q000737:chemistry; D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D003486:Cyanides / Q000378:metabolism; D019281:Dimerization; D016681:Genome, Fungal; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D016415:Sequence Alignment; D013379:Substrate Specificity; D000099170:Bis(5'-adenosyl)triphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000581:Amidohydrolases; D003486:Cyanides; D006867:Hydrolases; D009363:Neoplasm Proteins; D000099170:Bis(5'-adenosyl)triphosphatase; C080477:N-carbamoyl-D-amino acid amidohydrolase