|Protein Science (2006) 15(7):1735-44|
|New York Structural Genomics Research Consortium|
(click to unfold)
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.
|chemistry enzymology |
|Thermoplasma Protein Conformation Hydrolases Binding Sites Sequence Homology, Amino Acid Phosphoric Monoester Hydrolases |
|27 (Last update: 08/19/2017 11:16:08am)|
|Protein Sci. 2006 Jul;15(7):1735-44.|