1u02 | pdb_00001u02

File:1u02.gif

spinqualitylabelsall models 1u02, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Crystal structure of trehalose-6-phosphate phosphatase related protein

Overview

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.

About this Structure

1U02 is a Single protein structure of sequence from Thermoplasma acidophilum with MG, NA and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications., Rao KN, Kumaran D, Seetharaman J, Bonanno JB, Burley SK, Swaminathan S, Protein Sci. 2006 Jul;15(7):1735-44. PMID:16815921

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