1u02: Difference between revisions

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New page: left|200px<br /><applet load="1u02" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u02, resolution 1.92Å" /> '''Crystal structure of...
 
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[[Image:1u02.gif|left|200px]]<br /><applet load="1u02" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1u02.gif|left|200px]]<br /><applet load="1u02" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1u02, resolution 1.92&Aring;" />
caption="1u02, resolution 1.92&Aring;" />
'''Crystal structure of trehalose-6-phosphate phosphatase related protein'''<br />
'''Crystal structure of trehalose-6-phosphate phosphatase related protein'''<br />


==Overview==
==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.
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==
==About this Structure==
1U02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with MG, NA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U02 OCA].  
1U02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U02 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Burley, S.K.]]
[[Category: Burley, S K.]]
[[Category: Krishnamurthy, N.R.]]
[[Category: Krishnamurthy, N R.]]
[[Category: Kumaran, D.]]
[[Category: Kumaran, D.]]
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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Revision as of 13:19, 21 February 2008

File:1u02.gif


1u02, resolution 1.92Å

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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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