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dc.contributor.authorKrapp, Stephanen_US
dc.contributor.authorK. Münster-Kühnel, Anjaen_US
dc.contributor.authorKaiser, Jensen_US
dc.contributor.authorHuber, Roberten_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorJacob, Uween_US
dc.date.accessioned2017-04-24T11:32:22Z
dc.date.available2017-04-24T11:32:22Z
dc.date.issued2003en_US
dc.date.modified2009-02-27T06:44:00Z
dc.identifier.issn00222836en_US
dc.identifier.doi10.1016/j.jmb.2003.09.080en_AU
dc.identifier.urihttp://hdl.handle.net/10072/21481
dc.description.abstractSialic acids are activated by CMP-5-N-acetylneuraminic acid synthetase prior to their transfer onto oligo- or polysaccharides. Here, we present the crystal structure of the N-terminal catalytically active domain of the murine 5-N-acetylneuraminic acid synthetase in complex with the reaction product. In contrast to the previously solved structure of 5-N-acetylneuraminic acid synthetase from Neisseria meningitidis and the related CMP-KDO-synthetase of Escherichia coli, the murine enzyme is a tetramer, which was observed with the active sites closed. In this conformation a loop is shifted by 6 Štowards the active site and thus an essential arginine residue can participate in catalysis. Furthermore, a network of intermolecular salt-bridges and hydrogen bonds in the dimer as well as hydrophobic interfaces between two dimers indicate a cooperative behaviour of the enzyme. In addition, a complex regulation of the enzyme activity is proposed that includes phosphorylation and dephosphorylation.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.publisher.urihttp://www.sciencedirect.com/science/journal/00222836en_AU
dc.relation.ispartofpagefrom625en_US
dc.relation.ispartofpageto637en_US
dc.relation.ispartofissue4en_US
dc.relation.ispartofjournalJournal of Molecular Biologyen_US
dc.relation.ispartofvolume334en_US
dc.subject.fieldofresearchcode320302en_US
dc.subject.fieldofresearchcode270108en_US
dc.titleThe crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase.en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2003
gro.hasfulltextNo Full Text


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