The C-terminal region of xylanase domain in Xyn11A from Paenibacillus curdlanolyticus B-6 plays an important role in structural stability

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dc.contributor.authorJunjarus Sermsathanaswadi
dc.contributor.authorSomsak Pianwanit
dc.contributor.authorPatthra Pason
dc.contributor.authorRattiya Waeonukul
dc.contributor.authorChakrit Tachaapaikoon
dc.contributor.authorKhanok Ratanakhanokchai
dc.contributor.authorKrisna Septiningrum
dc.contributor.authorAkihiko Kosugi
dc.date.accessioned2025-03-10T07:37:40Z
dc.date.available2025-03-10T07:37:40Z
dc.date.issued2014
dc.description.abstractPaenibacillus curdlanolyticus B-6 produces an extracellular multienzyme complex containing a major xylanase subunit, designated Xyn11A, which includes two functional domains belonging to glycosyl hydrolase family-11 (GH11) and carbohydrate binding module family-36 (CBM36) and possesses a glycine and asparagine-rich linker (linker). To clarify the roles of each functional domain, recombinant proteins XynXL and XynX (CBM36 deleted and CBM36 and linker deleted, respectively) were constructed. Their xylanase activities were similar toward soluble xylan, whereas XynXL showed decreased hydrolysis activity toward insoluble xylan while XynX had no xylanase activity. To determine the significance of the linker and its neighbor region, XynX was subjected to secondary structural alignments using circular dichroism (CD) spectroscopy and three-dimensional (3D) structural analysis. A seven amino acid (NTITIGG) neighbor linker sequence was highly conserved among GH11 xylanases of Paenibacillus species. Although XynX exhibited a typical GH11 xylanase structure, conformational gaps were observed in the _6- and _12-sheets and in CD spectra. Flipping of the Arg163 side chains in the subsite was also observed upon analysis of superimposed models. Docking analysis using xylohexaose indicated that flipping of the Arg163 side chains markedly affected substrate binding in the subsite. To identify the amino acids related to stabilizing the substrate binding site, XynX with an extended C-terminal region was designed. At least seven amino acids were necessary to recover substrate binding and xylanase activity. These results indicated that the seven amino acid neighbor Xyn11A linker plays an important role in the activity and conformational stability of the xylanase domain. © 2014, Springer-Verlag Berlin Heidelberg.
dc.identifier.citationApplied Microbiology and Biotechnology
dc.identifier.doi10.1007/s00253-014-5748-x
dc.identifier.issn1757598
dc.identifier.scopus2-s2.0-84920253530
dc.identifier.urihttps://repository.dusit.ac.th//handle/123456789/4948
dc.languageEnglish
dc.publisherSpringer Verlag
dc.rights.holderScopus
dc.subjectCBM
dc.subjectGH family-11
dc.subjectPaenibacillus curdlanolyticus
dc.subjectXylan degradation
dc.subjectXylanase
dc.titleThe C-terminal region of xylanase domain in Xyn11A from Paenibacillus curdlanolyticus B-6 plays an important role in structural stability
dc.typeArticle
mods.location.urlhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84920253530&doi=10.1007%2fs00253-014-5748-x&partnerID=40&md5=18c82ad45067a4ba6e93aa07c3ed28d7
oaire.citation.endPage8233
oaire.citation.issue19
oaire.citation.startPage8223
oaire.citation.volume98
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