1U02

Crystal structure of trehalose-6-phosphate phosphatase related protein

Summary for 1U02

• Entry DOI: 10.2210/pdb1u02/pdb
• Descriptor: trehalose-6-phosphate phosphatase related protein, MAGNESIUM ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: structural genomics, phosphatase, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 1
• Total formula weight: 27773.74

Authors

Krishnamurthy, N.R.,Kumaran, D.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2004-07-12, release date: 2004-07-20, Last modification date: 2024-11-13)

Primary citation

Rao, K.N.,Kumaran, D.,Seetharaman, J.,Bonanno, J.B.,Burley, S.K.,Swaminathan, S.
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
Protein Sci., 15:1735-1744, 2006

PubMed 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 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.

PubMed: 16815921
DOI: 10.1110/ps.062096606

Experimental method

X-RAY DIFFRACTION (1.92 Å)