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| | <StructureSection load='2uwf' size='340' side='right'caption='[[2uwf]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2uwf' size='340' side='right'caption='[[2uwf]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2uwf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_alcalophilus_subsp._halodurans"_boyer_et_al._1973 "bacillus alcalophilus subsp. halodurans" boyer et al. 1973]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UWF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2uwf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans Alkalihalobacillus halodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UWF FirstGlance]. <br> |
| - | </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=CU:COPPER+(II)+ION'>CU</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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://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=CU:COPPER+(II)+ION'>CU</scene></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=2uwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwf OCA], [https://pdbe.org/2uwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwf RCSB], [https://www.ebi.ac.uk/pdbsum/2uwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwf 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=2uwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwf OCA], [https://pdbe.org/2uwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwf RCSB], [https://www.ebi.ac.uk/pdbsum/2uwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYNA_HALH5 XYNA_HALH5] |
| | == 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: Bacillus alcalophilus subsp. halodurans boyer et al. 1973]] | + | [[Category: Alkalihalobacillus halodurans]] |
| - | [[Category: Endo-1,4-beta-xylanase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hatti-Kaul, R]] | + | [[Category: Hatti-Kaul R]] |
| - | [[Category: Mamo, G]] | + | [[Category: Mamo G]] |
| - | [[Category: Mattiasson, B]] | + | [[Category: Mattiasson B]] |
| - | [[Category: Thunnissen, M]] | + | [[Category: Thunnissen M]] |
| - | [[Category: Alkaline adaptation]]
| + | |
| - | [[Category: Alkaliphilic]]
| + | |
| - | [[Category: Bacillus haloduran]]
| + | |
| - | [[Category: Endoxylanase]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Xylan degradation]]
| + | |
| - | [[Category: Xylanase structure]]
| + | |
| Structural highlights
Function
XYNA_HALH5
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 alkaliphilic bacterium, Bacillus halodurans S7, produces an alkaline active xylanase (EC 3.2.1.8), which differs from many other xylanases in being operationally stable under alkaline conditions as well as at elevated temperature. Compared to non-alkaline active xylanases, this enzyme has a high percent composition of acidic amino acids which results in high ratio of negatively to positively charged residues. A positive correlation was observed between the charge ratio and the pH optima of xylanases. The recombinant xylanase was crystallized using a hanging drop diffusion method. The crystals belong to the space group P2(1)2(1)2(1) and the structure was determined at a resolution of 2.1 A. The enzyme has the common eight-fold TIM-barrel structure of family 10 xylanases; however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft. Mutational analysis of non-conserved amino acids which are close to the acid/base residue has shown that Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH. Unlike the wild type xylanase which has optimum pH at 9-9.5, the triple mutant xylanase (V169A, I170F and D171N), which was constructed using sequence information of alkaline sensitive xylanses was optimally active around pH 7. Compared to non-alkaline active xylanases, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues. Based on these results obtained from sequence, structural and mutational analysis, the possible mechanisms of high pH stability and catalysis are discussed. This will provide useful information to understand the mechanism of high pH adaptation and engineering of enzymes that can be operationally stable at high pH.
An alkaline active xylanase: insights into mechanisms of high pH catalytic adaptation.,Mamo G, Thunnissen M, Hatti-Kaul R, Mattiasson B Biochimie. 2009 Sep;91(9):1187-96. Epub 2009 Jun 28. PMID:19567261[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mamo G, Thunnissen M, Hatti-Kaul R, Mattiasson B. An alkaline active xylanase: insights into mechanisms of high pH catalytic adaptation. Biochimie. 2009 Sep;91(9):1187-96. Epub 2009 Jun 28. PMID:19567261 doi:10.1016/j.biochi.2009.06.017
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