1qwj

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|PDB= 1qwj |SIZE=350|CAPTION= <scene name='initialview01'>1qwj</scene>, resolution 2.8&Aring;
|PDB= 1qwj |SIZE=350|CAPTION= <scene name='initialview01'>1qwj</scene>, resolution 2.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NCC:CYTIDINE-5&#39;-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC ACID'>NCC</scene>
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|LIGAND= <scene name='pdbligand=NCC:CYTIDINE-5&#39;-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC+ACID'>NCC</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|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])
 +
|DOMAIN=
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|RELATEDENTRY=[[1eyr|1EYR]], [[1gqc|1GQC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwj OCA], [http://www.ebi.ac.uk/pdbsum/1qwj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qwj RCSB]</span>
}}
}}
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[[Category: Muenster-Kuehnel, A K.]]
[[Category: Muenster-Kuehnel, A K.]]
[[Category: Tiralongo, J.]]
[[Category: Tiralongo, J.]]
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[[Category: NCC]]
 
[[Category: cmp-5-n-acetylneuraminic acid synthetase]]
[[Category: cmp-5-n-acetylneuraminic acid synthetase]]
[[Category: cmp-neu5ac]]
[[Category: cmp-neu5ac]]
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[[Category: sugar-activating enzyme]]
[[Category: sugar-activating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:24:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:56 2008''

Revision as of 20:19, 30 March 2008


PDB ID 1qwj

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands:
Gene: Cmas (Mus musculus)
Activity: N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43
Related: 1EYR, 1GQC


Resources: FirstGlance, OCA, PDBsum, RCSB
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

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