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| | ==Structure of uncomplexed Carbohydrate Binding Domain CBM36== | | ==Structure of uncomplexed Carbohydrate Binding Domain CBM36== |
| - | <StructureSection load='1w0n' size='340' side='right' caption='[[1w0n]], [[Resolution|resolution]] 0.80Å' scene=''> | + | <StructureSection load='1w0n' size='340' side='right'caption='[[1w0n]], [[Resolution|resolution]] 0.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w0n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacillus_polymyxa"_(prazmowski_1880)_donker_1926 "aerobacillus polymyxa" (prazmowski 1880) donker 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_polymyxa Paenibacillus polymyxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 0.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ux7|1ux7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></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=1w0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0n OCA], [https://pdbe.org/1w0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0n RCSB], [https://www.ebi.ac.uk/pdbsum/1w0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0n ProSAT]</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=1w0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0n OCA], [http://pdbe.org/1w0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0n RCSB], [http://www.ebi.ac.uk/pdbsum/1w0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/XYND_PAEPO XYND_PAEPO]] Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity. | + | [https://www.uniprot.org/uniprot/XYND_PAEPO XYND_PAEPO] Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Endo-1,4-beta-xylanase]] | + | [[Category: Large Structures]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Paenibacillus polymyxa]] |
| - | [[Category: Davies, G J]] | + | [[Category: Boraston AB]] |
| - | [[Category: Jamal, S]] | + | [[Category: Davies GJ]] |
| - | [[Category: Carbohydrate binding]] | + | [[Category: Jamal S]] |
| - | [[Category: Carbohydrate-binding module]]
| + | |
| - | [[Category: Cbm36]]
| + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Xylan]]
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| - | [[Category: Xylanase]]
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| Structural highlights
Function
XYND_PAEPO Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzymatic degradation of polysaccharides harnesses multimodular enzymes whose carbohydrate binding modules (CBM) target the catalytic domain onto the recalcitrant substrate. Here we report the ab initio structure determination and subsequent refinement, at 0.8 A resolution, of the CBM36 domain of the Paenibacillus polymyxa xylanase 43A. Affinity electrophoresis, isothermal titration calorimetry, and UV difference spectroscopy demonstrate that CBM36 is a novel Ca(2+)-dependent xylan binding domain. The 3D structure of CBM36 in complex with xylotriose and Ca(2+), at 1.5 A resolution, displays significant conformational changes compared to the native structure and reveals the molecular basis for its unique Ca(2+)-dependent binding of xylooligosaccharides through coordination of the O2 and O3 hydroxyls. CBM36 is one of an emerging spectrum of carbohydrate binding modules that increasingly find applications in industry and display great potential for mapping the "glyco-architecture" of plant cells.
Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules.,Jamal-Talabani S, Boraston AB, Turkenburg JP, Tarbouriech N, Ducros VM, Davies GJ Structure. 2004 Jul;12(7):1177-87. PMID:15242594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jamal-Talabani S, Boraston AB, Turkenburg JP, Tarbouriech N, Ducros VM, Davies GJ. Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules. Structure. 2004 Jul;12(7):1177-87. PMID:15242594 doi:10.1016/j.str.2004.04.022
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