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| ==Xsa43E, a GH43 family enzyme from Butyrivibrio proteoclasticus== | | ==Xsa43E, a GH43 family enzyme from Butyrivibrio proteoclasticus== |
- | <StructureSection load='4nov' size='340' side='right' caption='[[4nov]], [[Resolution|resolution]] 1.33Å' scene=''> | + | <StructureSection load='4nov' size='340' side='right'caption='[[4nov]], [[Resolution|resolution]] 1.33Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4nov]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NOV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NOV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Butyrivibrio_proteoclasticus_B316 Butyrivibrio proteoclasticus B316]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NOV 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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.33Å</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylan_1,4-beta-xylosidase Xylan 1,4-beta-xylosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.37 3.2.1.37] </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=4nov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nov OCA], [https://pdbe.org/4nov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nov RCSB], [https://www.ebi.ac.uk/pdbsum/4nov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nov 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=4nov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nov RCSB], [http://www.ebi.ac.uk/pdbsum/4nov PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| </div> | | </div> |
| + | <div class="pdbe-citations 4nov" style="background-color:#fffaf0;"></div> |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Xylan 1,4-beta-xylosidase]] | + | [[Category: Butyrivibrio proteoclasticus B316]] |
- | [[Category: Arcus, V L]] | + | [[Category: Large Structures]] |
- | [[Category: Till, M]] | + | [[Category: Arcus VL]] |
- | [[Category: Bladed beta-propellor]] | + | [[Category: Till M]] |
- | [[Category: Arabinofuranosidase]]
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- | [[Category: Hydrolase]]
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| Structural highlights
Publication Abstract from PubMed
The rumen of dairy cattle can be thought of as a large, stable fermentation vat and as such it houses a large and diverse community of microorganisms. The bacterium Butyrivibrio proteoclasticus is a representative of a significant component of this microbial community. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. This suite of enzymes is essential for the organism to utilize the plant material within the rumen as a fuel source, facilitating its survival in this competitive environment. Xsa43E, a GH43 enzyme from B. proteoclasticus, has been structurally and functionally characterized. Here, the structure of selenomethionine-derived Xsa43E determined to 1.3 A resolution using single-wavelength anomalous diffraction is reported. Xsa43E possesses the characteristic five-bladed beta-propeller domain seen in all GH43 enzymes. GH43 enzymes can have a range of functions, and the functional characterization of Xsa43E shows it to be an arabinofuranosidase capable of cleaving arabinose side chains from short segments of xylan. Full functional and structural characterization of xylan-degrading enzymes will aid in creating an enzyme cocktail that can be used to completely degrade plant material into simple sugars. These molecules have a range of applications as starting materials for many industrial processes, including renewable alternatives to fossil fuels.
Structural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus.,Till M, Goldstone D, Card G, Attwood GT, Moon CD, Arcus VL Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1193-8. doi:, 10.1107/S2053230X14014745. Epub 2014 Aug 29. PMID:25195890[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Till M, Goldstone D, Card G, Attwood GT, Moon CD, Arcus VL. Structural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1193-8. doi:, 10.1107/S2053230X14014745. Epub 2014 Aug 29. PMID:25195890 doi:http://dx.doi.org/10.1107/S2053230X14014745
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