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Crystal structure of trehalose‐6‐phosphate phosphatase–related protein: Biochemical and biological implications
Author(s) -
Rao Krishnamurthy N.,
Kumaran Desigan,
Seetharaman Jayaraman,
Bonanno Jeffrey B.,
Burley Stephen K.,
Swaminathan Subramanyam
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062096606
Subject(s) - phosphatase , trehalose , thermoplasma acidophilum , hydrolase , biochemistry , chemistry , protein structure , crystallography , biology , enzyme
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 α/β‐hydrolase fold, characteristic of the HAD family, and a cap domain, with a tertiary fold consisting of a four‐stranded β‐sheet with two α‐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.