The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase

Krapp, Stephan, Münster-Kühnel, Anja K., Kaiser, Jens T., Huber, Robert, Tiralongo, Joe, Gerardy-Schahn, Rita and Jacob, Uwe 2003. The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase. Journal of Molecular Biology 334 (4) , pp. 625-637. 10.1016/j.jmb.2003.09.080

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Abstract

Sialic 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 Å towards 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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Elsevier
ISSN:	0022-2836
Last Modified:	24 Jun 2017 11:00
URI:	https://orca.cardiff.ac.uk/id/eprint/70173

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