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| | <StructureSection load='5brq' size='340' side='right'caption='[[5brq]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5brq' size='340' side='right'caption='[[5brq]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5brq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacld Bacld]. 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> | + | <table><tr><td colspan='2'>[[5brq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis_DSM_13_=_ATCC_14580 Bacillus licheniformis DSM 13 = ATCC 14580]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5brq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5brq OCA], [https://pdbe.org/5brq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5brq RCSB], [https://www.ebi.ac.uk/pdbsum/5brq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5brq ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">treA, BL03069 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=279010 BACLD])</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5brq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q65MI2_BACLD Q65MI2_BACLD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha,alpha-phosphotrehalase]] | + | [[Category: Bacillus licheniformis DSM 13 = ATCC 14580]] |
| - | [[Category: Bacld]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hsiao, C D]] | + | [[Category: Hsiao C-D]] |
| - | [[Category: Lin, M G]] | + | [[Category: Lin M-G]] |
| - | [[Category: Gh13 family]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Trehalose-6-phosphate hydrolase]]
| + | |
| Structural highlights
Function
Q65MI2_BACLD
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lin MG, Chi MC, Naveen V, Li YC, Lin LL, Hsiao CD. Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity. Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):59-70. doi:, 10.1107/S2059798315020756. Epub 2016 Jan 1. PMID:26894535 doi:http://dx.doi.org/10.1107/S2059798315020756
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