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dc.contributor.authorOschlies, Melanie
dc.contributor.authorDickmanns, Achim
dc.contributor.authorHaselhorst, Thomas
dc.contributor.authorSchaper, Wiebke
dc.contributor.authorStummeyer, Katharina
dc.contributor.authorTiralongo, Joe
dc.contributor.authorWeinhold, Birgit
dc.contributor.authorGerardy-Schahn, Rita
dc.contributor.authorvon Itzstein, Mark
dc.contributor.authorFicner, Ralf
dc.contributor.authorMuenster-Kuehnel, Anja-K
dc.date.accessioned2017-05-03T15:42:29Z
dc.date.available2017-05-03T15:42:29Z
dc.date.issued2009
dc.date.modified2010-06-24T05:21:11Z
dc.identifier.issn0022-2836
dc.identifier.doi10.1016/j.jmb.2009.08.003
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom83
dc.relation.ispartofpageto97
dc.relation.ispartofissue1
dc.relation.ispartofjournalJournal of Molecular Biology
dc.relation.ispartofvolume393
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchCharacterisation of biological macromolecules
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode340403
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3107
dc.titleA C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2009
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark
gro.griffith.authorHaselhorst, Thomas E.
gro.griffith.authorTiralongo, Joe


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