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1qwj
From Proteopedia
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|PDB= 1qwj |SIZE=350|CAPTION= <scene name='initialview01'>1qwj</scene>, resolution 2.8Å | |PDB= 1qwj |SIZE=350|CAPTION= <scene name='initialview01'>1qwj</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NCC:CYTIDINE-5 | + | |LIGAND= <scene name='pdbligand=NCC:CYTIDINE-5'-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC ACID'>NCC</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/N-acylneuraminate_cytidylyltransferase N-acylneuraminate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.43 2.7.7.43] | |ACTIVITY= [http://en.wikipedia.org/wiki/N-acylneuraminate_cytidylyltransferase N-acylneuraminate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.43 2.7.7.43] | ||
|GENE= Cmas ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Cmas ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
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[[Category: sugar-activating enzyme]] | [[Category: sugar-activating enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:24:02 2008'' |
Revision as of 11:24, 23 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Cmas (Mus musculus) | ||||||
| Activity: | N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 23 13:24:02 2008
Categories: Mus musculus | N-acylneuraminate cytidylyltransferase | Single protein | Gerardy-Schahn, R. | Huber, R. | Jacob, U. | Kaiser, J T. | Krapp, S. | Muenster-Kuehnel, A K. | Tiralongo, J. | NCC | Cmp-5-n-acetylneuraminic acid synthetase | Cmp-neu5ac | Glycosylation | Lipopolysaccharide biosynthesis | Sialic acid | Sugar-activating enzyme
