Publication Abstract from PubMed
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 6A 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.
The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase.,Krapp S, Munster-Kuhnel AK, Kaiser JT, Huber R, Tiralongo J, Gerardy-Schahn R, Jacob U J Mol Biol. 2003 Dec 5;334(4):625-37. PMID:14636592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
