5brq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)== | |
| + | <StructureSection load='5brq' size='340' side='right' caption='[[5brq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5brq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BRQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5brp|5brp]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha,alpha-phosphotrehalase Alpha,alpha-phosphotrehalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.93 3.2.1.93] </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=5brq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5brq OCA], [http://pdbe.org/5brq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5brq RCSB], [http://www.ebi.ac.uk/pdbsum/5brq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Trehalose-6-phosphate hydrolase (TreA) belongs to glycoside hydrolase family 13 (GH13) and catalyzes the hydrolysis of trehalose 6-phosphate (T6P) to yield glucose and glucose 6-phosphate. The products of this reaction can be further metabolized by the energy-generating glycolytic pathway. Here, crystal structures of Bacillus licheniformis TreA (BlTreA) and its R201Q mutant complexed with p-nitrophenyl-alpha-D-glucopyranoside (R201Q-pPNG) are presented at 2.0 and 2.05 A resolution, respectively. The overall structure of BlTreA is similar to those of other GH13 family enzymes. However, detailed structural comparisons revealed that the catalytic site of BlTreA contains a long loop that adopts a different conformation from those of other GH13 family members. Unlike the homologous regions of Bacillus cereus oligo-1,6-glucosidase (BcOgl) and Erwinia rhapontici isomaltulose synthase (NX-5), the surface potential of the BlTreA active site exhibits a largely positive charge contributed by the four basic residues His281, His282, Lys284 and Lys292. Mutation of these residues resulted in significant decreases in the enzymatic activity of BlTreA. Strikingly, the (281)HHLK(284) motif and Lys292 play critical roles in substrate discrimination by BlTreA. | ||
| - | + | Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity.,Lin MG, Chi MC, Naveen V, Li YC, Lin LL, Hsiao CD Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):59-70. doi:, 10.1107/S2059798315020756. Epub 2016 Jan 1. PMID:26894535<ref>PMID:26894535</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Hsiao, C | + | <div class="pdbe-citations 5brq" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lin, M | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alpha,alpha-phosphotrehalase]] | ||
| + | [[Category: Hsiao, C D]] | ||
| + | [[Category: Lin, M G]] | ||
| + | [[Category: Gh13 family]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Tim barrel]] | ||
| + | [[Category: Trehalose-6-phosphate hydrolase]] | ||
Revision as of 14:58, 2 March 2016
Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)
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