title: Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
abstract: We report here the crystal structure of a trehalose-6-phosphate phosphatase-related protein (T6PP) from Thermoplasma acidophilum, TA1209, determined by the dual-wavelength anomalous diffraction (DAD) method. T6PP is a member of the haloacid dehalogenase (HAD) superfamily with significant sequence homology with trehalose-6-phosphate phosphatase, phosphoserine phosphatase, P-type ATPases and other members of the family. T6PP possesses a core domain of known alpha/beta-hydrolase fold, characteristic of the HAD family, and a cap domain, with a tertiary fold consisting of a four-stranded beta-sheet with two alpha-helices on one side of the sheet. An active-site magnesium ion and a glycerol molecule bound at the interface between the two domains provide insight into the mode of substrate binding by T6PP. A trehalose-6-phosphate molecule modeled into a cage formed by the two domains makes favorable interactions with the protein molecule. We have confirmed that T6PP is a trehalose phosphatase from amino acid sequence, three-dimensional structure, and biochemical assays.
authors.affiliation: Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
authors.forename: Krishnamurthy N
authors.initials: KN
authors.lastname: Rao
authors.forename: Desigan
authors.initials: D
authors.lastname: Kumaran
authors.forename: Jayaraman
authors.initials: J
authors.lastname: Seetharaman
authors.forename: Jeffrey B
authors.initials: JB
authors.lastname: Bonanno
authors.forename: Stephen K
authors.initials: SK
authors.lastname: Burley
authors.forename: Subramanyam
authors.initials: S
authors.lastname: Swaminathan
mesh_terms: D001665:Binding Sites; D006867:Hydrolases; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013822:Thermoplasma / Q000201:enzymology*
chemical_list: D006867:Hydrolases; C023178:trehalose-phosphatase; D010744:Phosphoric Monoester Hydrolases; C034507:2-haloacid dehalogenase