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| {{STRUCTURE_1u02| PDB=1u02 | SCENE= }} | | {{STRUCTURE_1u02| PDB=1u02 | SCENE= }} |
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| '''Crystal structure of trehalose-6-phosphate phosphatase related protein'''
| | ===Crystal structure of trehalose-6-phosphate phosphatase related protein=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16815921}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16815921 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16815921}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Psi]] | | [[Category: Psi]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:34:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:25:44 2008'' |
