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| | <StructureSection load='1u02' size='340' side='right'caption='[[1u02]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='1u02' size='340' side='right'caption='[[1u02]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U02 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U02 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U02 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ta1209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u02 OCA], [https://pdbe.org/1u02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u02 RCSB], [https://www.ebi.ac.uk/pdbsum/1u02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u02 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1u02 TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u02 OCA], [http://pdbe.org/1u02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u02 RCSB], [http://www.ebi.ac.uk/pdbsum/1u02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u02 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1u02 TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OTSBH_THEAC OTSBH_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).<ref>PMID:16815921</ref> | + | [https://www.uniprot.org/uniprot/OTSBH_THEAC OTSBH_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).<ref>PMID:16815921</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u0/1u02_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u0/1u02_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burley, S K]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Krishnamurthy, N R]] | + | [[Category: Burley SK]] |
| - | [[Category: Kumaran, D]] | + | [[Category: Krishnamurthy NR]] |
| - | [[Category: Structural genomic]] | + | [[Category: Kumaran D]] |
| - | [[Category: Swaminathan, S]] | + | [[Category: Swaminathan S]] |
| - | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
1u02 is a 1 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.92Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
OTSBH_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 PubMed
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.
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
- ↑ Rao KN, Kumaran D, Seetharaman J, Bonanno JB, Burley SK, Swaminathan S. Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications. Protein Sci. 2006 Jul;15(7):1735-44. PMID:16815921 doi:15/7/1735
- ↑ Rao KN, Kumaran D, Seetharaman J, Bonanno JB, Burley SK, Swaminathan S. Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications. Protein Sci. 2006 Jul;15(7):1735-44. PMID:16815921 doi:15/7/1735
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