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Protein Science (2006), 15:1735-1744. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Crystal structure of trehalose-6-phosphate phosphatase–related protein: Biochemical and biological implications

Krishnamurthy N. Rao1, Desigan Kumaran1, Jayaraman Seetharaman1, Jeffrey B. Bonanno2, Stephen K. Burley3 and Subramanyam Swaminathan1

1 Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA
2 New York Structural Biology Center, New York, New York 10027, USA
3 SGX Pharmaceuticals, Inc., San Diego, California 92121, USA

(RECEIVED January 24, 2006; FINAL REVISION March 30, 2006; ACCEPTED April 4, 2006)

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.

Keywords: enzymes; structure/function studies; structure; crystallography; protein structures; structural genomics; phosphatase


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