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

There are no files associated with this record.

Title The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase.
Author Krapp, Stephan; Münster-Kühnel, Anja K.; Kaiser, Jens; Huber, Robert; Tiralongo, Giuseppe; Gerardy-Schahn, Rita; Jacob, Uwe
Journal Name Journal of Molecular Biology
Year Published 2003
Place of publication United Kingdom
Publisher Elsevier
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.
Peer Reviewed Yes
Published Yes
Publisher URI http://www.sciencedirect.com/science/journal/00222836
Alternative URI http://dx.doi.org/10.1016/j.jmb.2003.09.080
Volume 334
Issue Number 4
Page from 625
Page to 637
ISSN 0022-2836
Date Accessioned 2006-06-29
Date Available 2009-02-27T06:44:00Z
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Enzymes; PRE2009-Medical Biochemistry: Carbohydrates
URI http://hdl.handle.net/10072/21481
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

Show simple item record

Griffith University copyright notice