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| | <StructureSection load='5t49' size='340' side='right'caption='[[5t49]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5t49' size='340' side='right'caption='[[5t49]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5t49]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bachd Bachd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T49 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5t49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T49 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.5Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t4a|5t4a]], [[5t4c|5t4c]], [[5t4g|5t4g]]</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=5t49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t49 OCA], [https://pdbe.org/5t49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t49 RCSB], [https://www.ebi.ac.uk/pdbsum/5t49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t49 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BH0236 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272558 BACHD])</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=5t49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t49 OCA], [http://pdbe.org/5t49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t49 RCSB], [http://www.ebi.ac.uk/pdbsum/5t49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t49 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/ENG1_HALH5 ENG1_HALH5] Cleaves internal linkages in 1,3-beta-glucan (PubMed:15501830, PubMed:28827308, PubMed:28781080). May contribute to plant biomass degradation (By similarity).[UniProtKB:Q47N06]<ref>PMID:15501830</ref> <ref>PMID:28781080</ref> <ref>PMID:28827308</ref> |
| - | Family 81 glycoside hydrolases (GHs), which are known to cleave beta-1,3-glucans, are found in archaea, bacteria, eukaryotes, and viruses. Here we examine the structural and functional features of the GH81 catalytic module, BhGH81, from the Bacillus halodurans protein BH0236 to probe the molecular basis of beta-1,3-glucan recognition and cleavage. BhGH81 displayed activity on laminarin, curdlan, and pachyman, but not scleroglucan; the enzyme also cleaved beta-1,3-glucooligosaccharides as small as beta-1,3-glucotriose. The crystal structures of BhGH81 in complex with various beta-1,3-glucooligosaccharides revealed distorted sugars in the -1 catalytic subsite and an arrangement consistent with an inverting catalytic mechanism having a proposed conformational itinerary of (2)S0 --> (2,5)B(double dagger) --> (5)S1. Notably, the architecture of the catalytic site, location of an adjacent ancillary beta-1,3-glucan binding site, and the surface properties of the enzyme indicate the likely ability to recognize the double and/or triple-helical quaternary structures adopted by beta-1,3-glucans.
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| - | Structural Analysis of a Family 81 Glycoside Hydrolase Implicates Its Recognition of beta-1,3-Glucan Quaternary Structure.,Pluvinage B, Fillo A, Massel P, Boraston AB Structure. 2017 Sep 5;25(9):1348-1359.e3. doi: 10.1016/j.str.2017.06.019. Epub, 2017 Aug 3. PMID:28781080<ref>PMID:28781080</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 5t49" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bachd]] | + | [[Category: Alkalihalobacillus halodurans C-125]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Pluvinage, B]] | + | [[Category: Pluvinage B]] |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
