Crystal structure of trehalose-6-phosphate phosphatase-related protein: Biochemical and biological implications

Krishnamurthy N. Rao, Desigan Kumaran, Jayaraman Seetharaman, Jeffrey B. Bonanno, Stephen K. Burley, Subramanyam Swaminathan

Research output: Contribution to journalArticle

41 Scopus citations

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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1735-1744
Number of pages10
JournalProtein Science
Volume15
Issue number7
DOIs
StatePublished - Jul 12 2006
Externally publishedYes

Keywords

  • Crystallography
  • Enzymes
  • Phosphatase
  • Protein structures
  • Structural genomics
  • Structure
  • Structure/function studies

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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