TY - JOUR
T1 - Crystal structure of trehalose-6-phosphate phosphatase-related protein
T2 - Biochemical and biological implications
AU - Rao, Krishnamurthy N.
AU - Kumaran, Desigan
AU - Seetharaman, Jayaraman
AU - Bonanno, Jeffrey B.
AU - Burley, Stephen K.
AU - Swaminathan, Subramanyam
PY - 2006
Y1 - 2006
N2 - 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. Published by Cold Spring Harbor Laboratory Press.
AB - 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. Published by Cold Spring Harbor Laboratory Press.
KW - Crystallography
KW - Enzymes
KW - Phosphatase
KW - Protein structures
KW - Structural genomics
KW - Structure
KW - Structure/function studies
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U2 - 10.1110/ps.062096606
DO - 10.1110/ps.062096606
M3 - Article
C2 - 16815921
AN - SCOPUS:33745712759
SN - 0961-8368
VL - 15
SP - 1735
EP - 1744
JO - Protein Science
JF - Protein Science
IS - 7
ER -