View source for 6qj6


==The structure of Trehalose-6-phosphatase from Burkholderia pseudomallei==
<StructureSection load='6qj6' size='340' side='right'caption='[[6qj6]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qj6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burps Burps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QJ6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">otsB, BPSL2411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272560 BURPS])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trehalose-phosphatase Trehalose-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.12 3.1.3.12] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qj6 OCA], [http://pdbe.org/6qj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qj6 RCSB], [http://www.ebi.ac.uk/pdbsum/6qj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qj6 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q63SB3_BURPS Q63SB3_BURPS]] Removes the phosphate from trehalose 6-phosphate to produce free trehalose.[RuleBase:RU361117] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the functional and structural characterization of trehalose-6-phosphate phosphatase (TPP), from the Gram-negative bacterium B. pseudomallei that causes melioidosis, a severe infectious disease endemic in Southeast Asia and Northern Australia. TPP is a key enzyme in the trehalose biosynthesis pathway, which plays an important role in bacterial stress responses. Due to the absence of this biosynthetic pathway in mammals, TPP has drawn attention as a potential drug target, to combat antibiotic resistance. In this context, we present a detailed biochemical analysis of purified recombinant TPP, reporting its specific high catalytic activity toward the trehalose-6-phosphate substrate, and an absolute requirement for its Mg(2+) cofactor. Furthermore, we present the crystal structure of TPP solved at 1.74 A, revealing the canonical haloacid dehalogenase (HAD) superfamily fold and conserved substrate binding pocket, from which insights into the catalytic mechanism may be deduced. Our data represent a starting point for the rational design of antibacterial drugs.

Functional and structural analysis of trehalose-6-phosphate phosphatase from Burkholderia pseudomallei: Insights into the catalytic mechanism.,Suthisawat S, Gourlay LJ, Bolognesi M, Boonyuen U, Vanaporn M Biochem Biophys Res Commun. 2020 Jan 20. pii: S0006-291X(20)30018-8. doi:, 10.1016/j.bbrc.2019.12.088. PMID:31973820<ref>PMID:31973820</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qj6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burps]]
[[Category: Large Structures]]
[[Category: Trehalose-phosphatase]]
[[Category: Gourlay, L J]]
[[Category: Hydrolase]]
[[Category: Trehalose-6-phosphatase]]