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dc.contributor.authorSteiner, Kerstin
dc.contributor.authorHageluken, Gregor
dc.contributor.authorMessner, Paul
dc.contributor.authorSchaeffer, Christina
dc.contributor.authorNaismith, James Henderson
dc.date.accessioned2013-08-05T12:01:01Z
dc.date.available2013-08-05T12:01:01Z
dc.date.issued2010-03-26
dc.identifier.citationSteiner , K , Hageluken , G , Messner , P , Schaeffer , C & Naismith , J H 2010 , ' Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus ' , Journal of Molecular Biology , vol. 397 , no. 2 , pp. 436-447 . https://doi.org/10.1016/j.jmb.2010.01.035en
dc.identifier.issn0022-2836
dc.identifier.otherPURE: 1908459
dc.identifier.otherPURE UUID: 1d492721-407c-40b5-a2f6-24e83ccbee67
dc.identifier.otherWOS: 000276273300007
dc.identifier.otherScopus: 77349090654
dc.identifier.urihttp://hdl.handle.net/10023/3906
dc.description.abstractCarbohydrate polymers are medically and industrially important. The S-layer of many Gram-positive organisms comprises protein and carbohydrate polymers and forms an almost paracrystalline array on the cell surface. Not only is this array important for the bacteria but it has potential application in the manufacture of commercially important polysaccharides and glycoconjugates as well. The S-layer glycoprotein glycan from Geobacillus stearothermophilus NRS 2004/3a is mainly composed of repeating units of three rhamnose sugars linked by alpha-1,3-, alpha-1,2-, and beta-1,2-linkages. The formation of the beta-1,2-linkage is catalysed by the enzyme WsaF. The rational use of this system is hampered by the fact that WsaF and other enzymes in the pathway share very little homology to other enzymes. We report the structural and biochemical characterisation of WsaF, the first such rhamnosyltransferase to be characterised. Structural work was aided by the surface entropy reduction method. The enzyme has two domains, the N-terminal domain, which binds the acceptor (the growing rhamnan chain), and the C-terminal domain, which binds the substrate (dTDP-beta-L-rhamnose). The structure of WsaF bound to dTDP and dTDP-beta-L-rhamnose coupled to biochemical analysis identifies the residues that underlie catalysis and substrate recognition. We have constructed and tested by site-directed mutagenesis a model for acceptor recognition. (C) 2010 Elsevier Ltd. All rights reserved.
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofJournal of Molecular Biologyen
dc.rightsCopyright © 2010 Elsevier Ltd.This is an open access article, available under a Creative Commons Licenceen
dc.subjectCrystal structureen
dc.subjectGeobacillus stearothermophilusen
dc.subjectRhamnosyltransferaseen
dc.subjectS-layer protein glycosylationen
dc.subjectGlycoprotein glycan Biosynthesisen
dc.subjectMannosyltreansferase pimaen
dc.subjectGlycogen-Synthaseen
dc.subjectDiffraction dataen
dc.subjectGene-clusteren
dc.subjectFamily GT4en
dc.subjectGlycosyltransferasesen
dc.subjectCatalysisen
dc.subjectSequenceen
dc.subjectQD Chemistryen
dc.subject.lccQDen
dc.titleStructural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilusen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1016/j.jmb.2010.01.035
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=77349090654&partnerID=8YFLogxKen


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