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dc.contributor.authorGoldston, David C.
dc.contributor.authorVillas-Bôas, Silas G
dc.contributor.authorTill, Marisa
dc.contributor.authorKelly, William J.
dc.contributor.authorAttwood, Graeme T.
dc.contributor.authorArcus, Vickery L.
dc.coverage.spatialUnited Statesen_NZ
dc.date.accessioned2010-02-22T01:32:34Z
dc.date.available2010-02-22T01:32:34Z
dc.date.issued2010
dc.identifier.citationGoldston, D. C., Villas-Boas, S. G., Till, M., Kelly, W. J., Attwood, G. T. & Arcus, V. L. (2010). Structural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticus. Proteins: Structure, Function, and Bioinformatics.en
dc.identifier.urihttps://hdl.handle.net/10289/3631
dc.description.abstractThe release of polysaccharide from the plant cell wall is a key process to release the stored energy from plant biomass. Within the ruminant digestive system, a host of commensal microorganisms speed the breakdown of plant cell matter releasing fermentable sugars. The presence of phenolic compounds, most notably ferulic acid (FA), esterified within the cell wall is thought to pose a significant impediment to the degradation of the plant cell wall. The structure of a FA esterase from the ruminant bacterium Butyrivibrio proteoclasticus has been determined in two different space groups, in both the apo-form, and the ligand bound form with FA located in the active site. The structure reveals a new lid domain that has no structural homologues in the PDB. The flexibility of the lid domain is evident by the presence of three different conformations adopted by different molecules in the crystals. In the FA-bound structures, these conformations show sequential binding and closing of the lid domain over the substrate. Enzymatic activity assays demonstrate a broad activity against plant-derived hemicellulose, releasing at least four aromatic compounds including FA, coumaric acid, coumarin-3-carboxylic acid, and cinnamic acid. The rumen is a complex ecosystem that efficiently degrades plant biomass and the genome of B. proteoclasticus contains greater than 130 enzymes, which are potentially involved in this process of which Est1E is the first to be well characterized.en
dc.language.isoen
dc.publisherWiley-Liss, Incen_NZ
dc.relation.urihttp://www3.interscience.wiley.com/journal/123190709/abstract?CRETRY=1&SRETRY=0en
dc.subjectrumenen
dc.subjectesteraseen
dc.subjectlid domainen
dc.subjectferulic aciden
dc.subjecthemicellulosesen
dc.subjectα/β- hydrolaseen
dc.titleStructural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticusen
dc.typeJournal Articleen
dc.identifier.doi10.1002/prot.22662en
dc.relation.isPartOfProteinsen_NZ
pubs.begin-page1en_NZ
pubs.elements-id34666
pubs.end-page13en_NZ
pubs.issue6en_NZ
pubs.volumeOnlineen_NZ


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