Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
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.
Rao
Krishnamurthy N
KN
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Kumaran
Desigan
D
Seetharaman
Jayaraman
J
Bonanno
Jeffrey B
JB
Burley
Stephen K
SK
Swaminathan
Subramanyam
S
D001665:Binding Sites; D006867:Hydrolases; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013822:Thermoplasma / Q000201:enzymology*
D006867:Hydrolases; C023178:trehalose-phosphatase; D010744:Phosphoric Monoester Hydrolases; C034507:2-haloacid dehalogenase