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1qwj

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(New page: 200px<br /><applet load="1qwj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwj, resolution 2.8&Aring;" /> '''The Crystal Structure...)
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Revision as of 22:56, 20 November 2007


1qwj, resolution 2.8Å

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The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase

Overview

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.

About this Structure

1QWJ is a Single protein structure of sequence from Mus musculus with NCC as ligand. Active as N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43 Full crystallographic information is available from OCA.

Reference

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

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