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

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Krapp, S
Munster-Kuhnel, AK
Kaiser, JT
Huber, R
Tiralongo, J
Gerardy-Schahn, R
Jacob, U
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2003
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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 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.

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Journal of Molecular Biology

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334

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4

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Medicinal and biomolecular chemistry

Biochemistry and cell biology

Microbiology

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