1u02

<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>

</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>

<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='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'>[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>

[[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>

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== 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<ref>PMID:16815921</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1u02" style="background-color:#fffaf0;"></div>

[[Category: Burley, S K]]

[[Category: Krishnamurthy, N R]]

[[Category: Kumaran, D]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: PSI, Protein structure initiative]]