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dc.contributor.authorOschlies, Melanieen_US
dc.contributor.authorDickmanns, Achimen_US
dc.contributor.authorHaselhorst, Thomasen_US
dc.contributor.authorSchaper, Wiebkeen_US
dc.contributor.authorStummeyer, Katharinaen_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorWeinhold, Birgiten_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.contributor.authorFicner, Ralfen_US
dc.contributor.authorMunster-Kuhnel, Anja-K.en_US
dc.date.accessioned2017-04-24T13:16:04Z
dc.date.available2017-04-24T13:16:04Z
dc.date.issued2009en_US
dc.date.modified2010-06-24T05:21:11Z
dc.identifier.issn00222836en_US
dc.identifier.doi10.1016/j.jmb.2009.08.003en_AU
dc.identifier.urihttp://hdl.handle.net/10072/30542
dc.description.abstractThe biosynthesis of sialic acid-containing glycoconjugates is crucial for the development of vertebrate life. Cytidine monophosphate-sialic acid synthetase (CSS) catalyzes the metabolic activation of sialic acids. In vertebrates, the enzyme is chimeric, with the N-terminal domain harboring the synthetase activity. The function of the highly conserved C-terminal domain (CSS-CT) is unknown. To shed light on its biological function, we solved the X-ray structure of murine CSS-CT to 1.9 Šresolution. CSS-CT is a stable shamrock-like tetramer that superimposes well with phosphatases of the haloacid dehalogenase superfamily. However, a region found exclusively in vertebrate CSS-CT appears to block the active-site entrance. Accordingly, no phosphatase activity was observed in vitro, which points toward a nonenzymatic function of CSS-CT. A computational three-dimensional model of full-length CSS, in combination with in vitro oligomerization studies, provides evidence that CSS-CT serves as a platform for the quaternary organization governing the kinetic properties of the physiologically active enzyme as demonstrated in kinetic studies.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom83en_US
dc.relation.ispartofpageto97en_US
dc.relation.ispartofissue1en_US
dc.relation.ispartofjournalJournal of Molecular Biologyen_US
dc.relation.ispartofvolume393en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchCharacterisation of Biological Macromoleculesen_US
dc.subject.fieldofresearchcode030403en_US
dc.titleA C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzymeen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2009
gro.hasfulltextNo Full Text


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