1qwj: Difference between revisions
New page: left|200px<br /><applet load="1qwj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwj, resolution 2.8Å" /> '''The Crystal Structure... |
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[[Image:1qwj.gif|left|200px]]<br /><applet load="1qwj" size=" | [[Image:1qwj.gif|left|200px]]<br /><applet load="1qwj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qwj, resolution 2.8Å" /> | caption="1qwj, resolution 2.8Å" /> | ||
'''The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase'''<br /> | '''The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase'''<br /> | ||
==Overview== | ==Overview== | ||
Sialic acids are activated by CMP-5-N-acetylneuraminic acid synthetase | 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== | ==About this Structure== | ||
1QWJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NCC as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1QWJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NCC:'>NCC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Jacob, U.]] | [[Category: Jacob, U.]] | ||
[[Category: Kaiser, J | [[Category: Kaiser, J T.]] | ||
[[Category: Krapp, S.]] | [[Category: Krapp, S.]] | ||
[[Category: Muenster-Kuehnel, A | [[Category: Muenster-Kuehnel, A K.]] | ||
[[Category: Tiralongo, J.]] | [[Category: Tiralongo, J.]] | ||
[[Category: NCC]] | [[Category: NCC]] | ||
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[[Category: sugar-activating enzyme]] | [[Category: sugar-activating enzyme]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:27 2008'' | ||
Revision as of 12:44, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 14:44:27 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
