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| | <StructureSection load='5k9y' size='340' side='right'caption='[[5k9y]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5k9y' size='340' side='right'caption='[[5k9y]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k9y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k9y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9Y FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xynA, BSU18840 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</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=5k9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9y OCA], [https://pdbe.org/5k9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9y RCSB], [https://www.ebi.ac.uk/pdbsum/5k9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9y 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=5k9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9y OCA], [http://pdbe.org/5k9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9y RCSB], [http://www.ebi.ac.uk/pdbsum/5k9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYNA_BACSU XYNA_BACSU] |
| | <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: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Endo-1,4-beta-xylanase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ferreira, T L]] | + | [[Category: Ferreira TL]] |
| - | [[Category: Fuzo, C A]] | + | [[Category: Fuzo CA]] |
| - | [[Category: Lourenzoni, M R]] | + | [[Category: Lourenzoni MR]] |
| - | [[Category: Nonato, M C]] | + | [[Category: Nonato MC]] |
| - | [[Category: Pinheiro, M P]] | + | [[Category: Pinheiro MP]] |
| - | [[Category: Silva, S R]] | + | [[Category: Silva SR]] |
| - | [[Category: Silva, S R.B]] | + | [[Category: Silva SRB]] |
| - | [[Category: Vieira, D S]] | + | [[Category: Vieira DS]] |
| - | [[Category: Ward, R J]] | + | [[Category: Ward RJ]] |
| - | [[Category: 4-beta-xylanase some]]
| + | |
| - | [[Category: Endo-1]]
| + | |
| - | [[Category: Glycoside hydrolase family 11]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thermostability]]
| + | |
| Structural highlights
Function
XYNA_BACSU
Publication Abstract from PubMed
A thermostable variant of the mesophilic xylanase A from Bacillus subtilis (BsXynA-G3_4x) contains the four mutations Gln7His, Gly13Arg, Ser22Pro, and Ser179Cys. The crystal structure of the BsXynA-G3_4x has been solved, and the local environments around each of these positions investigated by molecular dynamics (MD) simulations at 328K and 348K. The structural and MD simulation results were correlated with thermodynamic data of the wild-type enzyme, the 4 single mutants and the BsXynA-G3_4x. This analysis suggests that the overall stabilizing effect is entropic, and is consistent with solvation of charged residues and reduction of main-chain flexibility. Furthermore, increased protein-protein hydrogen bonding and hydrophobic interactions also contribute to stabilize the BsXynA-G3_4x. The study revealed that a combination of several factors is responsible for increased thermostability of the BsXynA-G3_4x; (i) introduction of backbone rigidity in regions of high flexibility, (ii) solvation effects and (iii) hydrophobic contacts.
The role of local residue environmental changes in thermostable mutants of the GH11 xylanase from Bacillus subtilis.,Silva SB, Pinheiro MP, Fuzo CA, Silva SR, Ferreira TL, Lourenzoni MR, Nonato MC, Vieira DS, Ward RJ Int J Biol Macromol. 2017 Apr;97:574-584. doi: 10.1016/j.ijbiomac.2017.01.054., Epub 2017 Jan 18. PMID:28109807[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Silva SB, Pinheiro MP, Fuzo CA, Silva SR, Ferreira TL, Lourenzoni MR, Nonato MC, Vieira DS, Ward RJ. The role of local residue environmental changes in thermostable mutants of the GH11 xylanase from Bacillus subtilis. Int J Biol Macromol. 2017 Apr;97:574-584. doi: 10.1016/j.ijbiomac.2017.01.054., Epub 2017 Jan 18. PMID:28109807 doi:http://dx.doi.org/10.1016/j.ijbiomac.2017.01.054
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