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| | <StructureSection load='6ife' size='340' side='right'caption='[[6ife]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6ife' size='340' side='right'caption='[[6ife]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ife]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_7061 Atcc 7061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IFE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ife]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IFE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.804Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4107_1875 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1408 ATCC 7061])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6ife FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ife OCA], [https://pdbe.org/6ife PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ife RCSB], [https://www.ebi.ac.uk/pdbsum/6ife PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ife 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=6ife FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ife OCA], [http://pdbe.org/6ife PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ife RCSB], [http://www.ebi.ac.uk/pdbsum/6ife PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ife ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A4V8GZZ0_BACPU A0A4V8GZZ0_BACPU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ife" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ife" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Xylosidase 3D structures|Xylosidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 7061]] | + | [[Category: Bacillus pumilus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xylan 1,4-beta-xylosidase]]
| + | [[Category: Huang ZX]] |
| - | [[Category: Huang, Z X]] | + | [[Category: Li N]] |
| - | [[Category: Li, N]] | + | [[Category: Liu Y]] |
| - | [[Category: Liu, Y]] | + | [[Category: Zhang R]] |
| - | [[Category: Zhang, R]] | + | [[Category: Zhou JP]] |
| - | [[Category: Zhou, J P]] | + | |
| - | [[Category: Beta-xylosidase]]
| + | |
| - | [[Category: Glycoside hydrolase family 43]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Low-temperature activity]]
| + | |
| - | [[Category: Salt tolerance]]
| + | |
| Structural highlights
Function
A0A4V8GZZ0_BACPU
Publication Abstract from PubMed
beta-Xylosidase, of the glycoside hydrolase family 43 from Bacillus sp. HJ14, was expressed in Escherichia coli. Recombinant beta-xylosidase (rHJ14GH43) exhibited maximum activity at 25 degrees C, approximately 15, 45, and 88% of maximum activity at 0, 10, and 20 degrees C, respectively, and poor stability at temperatures over 20 degrees C. rHJ14GH43 showed moderate or high activity, but poor stability, in NaCl, KCl, NaNO3, KNO3, Na2SO4, and (NH4)2SO4 at concentrations from 3.0 to 30.0% (w/v). The crystal structure of rHJ14GH43 was resolved and showed higher structural flexibility due to fewer salt bridges and hydrogen bonds compared to mesophilic and thermophilic beta-xylosidases. High structural flexibility is presumed to be a key factor for catalytic adaptations to low temperatures and high salt concentrations. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments.
Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 beta-xylosidase: Activity and instability at high neutral salt concentrations.,Zhang R, Li N, Liu Y, Han X, Tu T, Shen J, Xu S, Wu Q, Zhou J, Huang Z Food Chem. 2019 Dec 15;301:125266. doi: 10.1016/j.foodchem.2019.125266. Epub 2019, Jul 27. PMID:31387037[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang R, Li N, Liu Y, Han X, Tu T, Shen J, Xu S, Wu Q, Zhou J, Huang Z. Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 beta-xylosidase: Activity and instability at high neutral salt concentrations. Food Chem. 2019 Dec 15;301:125266. doi: 10.1016/j.foodchem.2019.125266. Epub 2019, Jul 27. PMID:31387037 doi:http://dx.doi.org/10.1016/j.foodchem.2019.125266
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