1u02
Crystal structure of trehalose-6-phosphate phosphatase related protein
Structural highlights
FunctionOTSBH_THEAC Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of para-nitrophenyl phosphate (pNPP), but with lesser efficiency (in vitro).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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