dc.contributor.author | Oschlies, Melanie | |
dc.contributor.author | Dickmanns, Achim | |
dc.contributor.author | Haselhorst, Thomas | |
dc.contributor.author | Schaper, Wiebke | |
dc.contributor.author | Stummeyer, Katharina | |
dc.contributor.author | Tiralongo, Joe | |
dc.contributor.author | Weinhold, Birgit | |
dc.contributor.author | Gerardy-Schahn, Rita | |
dc.contributor.author | von Itzstein, Mark | |
dc.contributor.author | Ficner, Ralf | |
dc.contributor.author | Muenster-Kuehnel, Anja-K | |
dc.date.accessioned | 2017-05-03T15:42:29Z | |
dc.date.available | 2017-05-03T15:42:29Z | |
dc.date.issued | 2009 | |
dc.date.modified | 2010-06-24T05:21:11Z | |
dc.identifier.issn | 0022-2836 | |
dc.identifier.doi | 10.1016/j.jmb.2009.08.003 | |
dc.identifier.uri | http://hdl.handle.net/10072/30542 | |
dc.description.abstract | The 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.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Elsevier | |
dc.publisher.place | United Kingdom | |
dc.relation.ispartofstudentpublication | N | |
dc.relation.ispartofpagefrom | 83 | |
dc.relation.ispartofpageto | 97 | |
dc.relation.ispartofissue | 1 | |
dc.relation.ispartofjournal | Journal of Molecular Biology | |
dc.relation.ispartofvolume | 393 | |
dc.rights.retention | Y | |
dc.subject.fieldofresearch | Medicinal and biomolecular chemistry | |
dc.subject.fieldofresearch | Characterisation of biological macromolecules | |
dc.subject.fieldofresearch | Biochemistry and cell biology | |
dc.subject.fieldofresearch | Microbiology | |
dc.subject.fieldofresearchcode | 3404 | |
dc.subject.fieldofresearchcode | 340403 | |
dc.subject.fieldofresearchcode | 3101 | |
dc.subject.fieldofresearchcode | 3107 | |
dc.title | A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
gro.date.issued | 2009 | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | von Itzstein, Mark | |
gro.griffith.author | Haselhorst, Thomas E. | |
gro.griffith.author | Tiralongo, Joe | |