Structural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus

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dc.contributor.authorTill, Marisa
dc.contributor.authorGoldstone, D.
dc.contributor.authorCard, G.
dc.contributor.authorAttwood, Graeme T.
dc.contributor.authorMoon, Christina D.
dc.contributor.authorArcus, Vickery L.
dc.coverage.spatialUnited Statesen_NZ
dc.date.accessioned2014-12-10T22:35:44Z
dc.date.available2014-08-29
dc.date.available2014-12-10T22:35:44Z
dc.date.issued2014-08-29
dc.description.abstractThe rumen of dairy cattle can be thought of as a large, stable fermentation vat and as such it houses a large and diverse community of microorganisms. The bacterium Butyrivibrio proteoclasticus is a representative of a significant component of this microbial community. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. This suite of enzymes is essential for the organism to utilize the plant material within the rumen as a fuel source, facilitating its survival in this competitive environment. Xsa43E, a GH43 enzyme from B. proteoclasticus, has been structurally and functionally characterized. Here, the structure of selenomethionine-derived Xsa43E determined to 1.3 Å resolution using single-wavelength anomalous diffraction is reported. Xsa43E possesses the characteristic five-bladed β-propeller domain seen in all GH43 enzymes. GH43 enzymes can have a range of functions, and the functional characterization of Xsa43E shows it to be an arabinofuranosidase capable of cleaving arabinose side chains from short segments of xylan. Full functional and structural characterization of xylan-degrading enzymes will aid in creating an enzyme cocktail that can be used to completely degrade plant material into simple sugars. These molecules have a range of applications as starting materials for many industrial processes, including renewable alternatives to fossil fuels.
dc.format.extent1193 - 1198
dc.format.mimetypeapplication/pdf
dc.identifier.citationTill, M., Goldstone, D., Card, G., Attwood, G. T., Moon, C. D., & Arcus, V. L. (2014). Structural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus. Acta Crystallographica Section F: Structural Biology Communications, 70(9), 1193–1198. http://doi.org/10.1107/S2053230X14014745en
dc.identifier.doi10.1107/S2053230X14014745
dc.identifier.issn2053-230X
dc.identifier.urihttps://hdl.handle.net/10289/8949
dc.languageeng
dc.publisherWiley-Blackwell
dc.relation.isPartOfActa Crystallographica Section F: Structural Biology Communications
dc.rights© International Union of Crystallography.
dc.subjectButyrivibrio proteoclasticus
dc.subjectGH43
dc.subjectXsa43E
dc.titleStructural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus
dc.typeJournal Article
pubs.begin-page1193
pubs.elements-id114805
pubs.end-page1198
pubs.issue9
pubs.notesEBSCOhost confirms peer reviewed
pubs.organisational-group/Waikato
pubs.organisational-group/Waikato/FSEN
pubs.organisational-group/Waikato/FSEN/School of Science
pubs.organisational-group/Waikato/FSEN/School of Science/Biological Sciences
pubs.volume70
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