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| | ==Structure of the N-terminal CBM22-1-CBM22-2 tandem domain from Paenibacillus barcinonensis Xyn10C== | | ==Structure of the N-terminal CBM22-1-CBM22-2 tandem domain from Paenibacillus barcinonensis Xyn10C== |
| - | <StructureSection load='4xup' size='340' side='right' caption='[[4xup]], [[Resolution|resolution]] 2.43Å' scene=''> | + | <StructureSection load='4xup' size='340' side='right'caption='[[4xup]], [[Resolution|resolution]] 2.43Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xup]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XUP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xup]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_barcinonensis Paenibacillus barcinonensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XUP 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=GOL:GLYCEROL'>GOL</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]] 2.43Å</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='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=GOL:GLYCEROL'>GOL</scene></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=4xup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xup OCA], [http://pdbe.org/4xup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xup RCSB], [http://www.ebi.ac.uk/pdbsum/4xup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xup ProSAT]</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=4xup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xup OCA], [https://pdbe.org/4xup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xup RCSB], [https://www.ebi.ac.uk/pdbsum/4xup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xup ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYNC_PAEBA XYNC_PAEBA] |
| | <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: Endo-1,4-beta-xylanase]] | + | [[Category: Large Structures]] |
| - | [[Category: Sainz-Polo, M A]] | + | [[Category: Paenibacillus barcinonensis]] |
| - | [[Category: Sanz-Aparicio, J]] | + | [[Category: Sainz-Polo MA]] |
| - | [[Category: 4-beta-xylanase]] | + | [[Category: Sanz-Aparicio J]] |
| - | [[Category: Binding site]]
| + | |
| - | [[Category: Carbohydrate]]
| + | |
| - | [[Category: Endo-1]]
| + | |
| - | [[Category: Enzyme stability]]
| + | |
| - | [[Category: Substrate specificity]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Thermophilic enzyme]]
| + | |
| - | [[Category: Thermostabilizing domain]]
| + | |
| - | [[Category: Xylan-binding domain]]
| + | |
| Structural highlights
Function
XYNC_PAEBA
Publication Abstract from PubMed
Elucidating the molecular mechanisms regulating multimodularity is a challenging task. Paenibacillus barcinonensis Xyn10C is a 120 kD modular enzyme that presents the CBM22/GH10/CBM9 architecture found in a subset of large xylanases. We report here the three-dimensional structure of the Xyn10C N-terminal region, containing the xylan-binding CBM22-1-CBM22-2 tandem (Xyn10C-XBD), which represents the first solved crystal structure of two contiguous CBM22. Xyn10C-XBD is folded into two separate CBM22 modules linked by a flexible segment that endows the tandem with extraordinary plasticity. Each isolated domain have been expressed and crystallized and their binding abilities have been investigated. Both domains contain the RW/YYYE motif required for xylan binding. However, crystallographic analysis of CBM22-2 complexes shows Trp308 as an additional binding determinant. The long loop containing Trp308 creates a platform that possibly contributes to recognize precise decorations at subsite S2. CBM22-2 may thus define a subset of xylan-binding CBM22s directed to particular regions of the polysaccharide. Affinity electrophoresis reveals Xyn10C-XBD binds arabinoxylans more tightly, more apparent when CBM22-2 is tested against highly substituted xylan. The crystal structure of the catalytic domain, also reported, shows the capacity of the active site to accommodate xylan substitutions at almost all subsites. The structural differences found at both Xyn10C-XBD domains are consistent with the ITC experiments showing two sites with different affinities in the tandem. On the basis of the CBM22 distinct characteristics, a deliver strategy of Xyn10C mediated by Xyn10C-XBD is proposed.
Exploring multimodularity in plant cell wall deconstruction: structural and functional analysis of Xyn10C containing the CBM22-1-CBM22-2 tandem.,Sainz-Polo MA, Gonzalez B, Menendez M, Pastor FI, Sanz-Aparicio J J Biol Chem. 2015 May 22. pii: jbc.M115.659300. PMID:26001782[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sainz-Polo MA, Gonzalez B, Menendez M, Pastor FI, Sanz-Aparicio J. Exploring multimodularity in plant cell wall deconstruction: structural and functional analysis of Xyn10C containing the CBM22-1-CBM22-2 tandem. J Biol Chem. 2015 May 22. pii: jbc.M115.659300. PMID:26001782 doi:http://dx.doi.org/10.1074/jbc.M115.659300
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