View source for 22gt


==a novel GH8 family xylanase BiXyn8A==
<StructureSection load='22gt' size='340' side='right'caption='[[22gt]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22gt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_intestinalis_DSM_17393 Bacteroides intestinalis DSM 17393]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22GT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22GT 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]] 1.8000029&#8491;</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=22gt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22gt OCA], [https://pdbe.org/22gt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22gt RCSB], [https://www.ebi.ac.uk/pdbsum/22gt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22gt ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside hydrolase family 8 (GH8) xylanases exhibit substantial diversity in catalytic mode and product distribution, yet the structural basis underlying this functional divergence remains poorly understood. Here, we report the identification and characterization of BgXyn8A, a GH8 xylanase from Bacillus glycinifermentans that exhibits a distinct preference for endo-type cleavage. BgXyn8A hydrolyzes xylan and alkali-pretreated corncob into a broad spectrum of xylooligosaccharides (XOSs) with degrees of polymerization ranging from 2 to 10, without detectable xylose formation. Comparative structural analysis with the exo-biased homolog BiXyn8A demonstrated that differences in product specificity are not governed by catalytic residues but arise from non-catalytic structural features surrounding the substrate-binding cleft. Specifically, three beta-sheet-rich peripheral regions form a rigid substrate-binding cleft that constrains substrate positioning and limits conformational flexibility, thereby favoring internal cleavage and early product release. In addition, a short entrance motif reduces stabilizing interactions with the substrate's reducing end, disfavoring iterative cleavage required for xylose formation. Consistently, transplantation of these features into BiXyn8A reprograms its product spectrum toward longer-chain XOSs while suppressing xylose production. This study extends the current structural understanding of GH8 xylanases and provides a foundation for the rational engineering of enzymes tailored for selective oligosaccharide production.

Biochemical and structural characterization of a novel glycoside hydrolase family 8 endoxylanase with broad-spectrum xylooligosaccharide production.,Liu Y, Xie W, Zhang Y, Liang S, Wang S, Zhan R, Wang C, Wang K Bioresour Technol. 2026 May 3;454:134780. doi: 10.1016/j.biortech.2026.134780. PMID:42086152<ref>PMID:42086152</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 22gt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacteroides intestinalis DSM 17393]]
[[Category: Large Structures]]
[[Category: Wei X]]
[[Category: Yun L]]