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7eo6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure analysis of xylanase== | |
| + | <StructureSection load='7eo6' size='340' side='right'caption='[[7eo6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7eo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomycetia_bacterium Actinomycetia bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=7eo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo6 OCA], [https://pdbe.org/7eo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo6 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2W4QIY3_9ACTN A0A2W4QIY3_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Xylanase is efficient for xylan degradation and widely applied in industries. We found a GH11 family xylanase (Xyn11A) with high thermostability and catalytic activity from compost metatranscriptome. This xylanase has the optimal reaction temperature at 80 degrees C with the activity of 2907.3 U/mg. The X-ray crystallographic structure shows a typical "right hand" architecture, which is the characteristics of the GH11 family enzymes. Comparing it with the mesophilic XYN II, a well-studied GH11 xylanase from Trichoderma reesei, Xyn11A is more compact with more H-bonds. Our mutagenic results show that the electrostatic interactions in the thumb and palm region of Xyn11A could result in its high thermostability and activity. Introducing a disulfide bond at the N-terminus further increased its optimal reaction temperature to 90 degrees C with augmented activity. KEY POINTS: * A hyperthermophilic xylanase with high activity was discovered using the metatranscriptomic method. * The mechanisms of thermophilicity and high activity were revealed using X-ray crystallography, mutagenesis, and molecular dynamics simulations. * The thermostability and activity were further improved by introducing a disulfide bond. | ||
| - | + | Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome.,Yi Y, Xu S, Kovalevsky A, Zhang X, Liu D, Wan Q Appl Microbiol Biotechnol. 2021 Oct;105(20):7757-7767. doi:, 10.1007/s00253-021-11587-2. Epub 2021 Sep 23. PMID:34553251<ref>PMID:34553251</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Wan | + | <div class="pdbe-citations 7eo6" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinomycetia bacterium]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wan Q]] | ||
| + | [[Category: Xu S]] | ||
| + | [[Category: Yi Y]] | ||
Current revision
X-ray structure analysis of xylanase
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