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[[Image:1qwj.gif|left|200px]]


{{Structure
==The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase==
|PDB= 1qwj |SIZE=350|CAPTION= <scene name='initialview01'>1qwj</scene>, resolution 2.8&Aring;
<StructureSection load='1qwj' size='340' side='right'caption='[[1qwj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NCC:CYTIDINE-5'-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC ACID'>NCC</scene>
<table><tr><td colspan='2'>[[1qwj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWJ FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE= Cmas ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCC:CYTIDINE-5-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC+ACID'>NCC</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwj OCA], [https://pdbe.org/1qwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwj RCSB], [https://www.ebi.ac.uk/pdbsum/1qwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwj ProSAT]</span></td></tr>
 
</table>
'''The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase'''
== Function ==
 
[https://www.uniprot.org/uniprot/NEUA_MOUSE NEUA_MOUSE] Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).<ref>PMID:9689047</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qwj_consurf.spt"</scriptWhenChecked>
1QWJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWJ OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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:[http://www.ncbi.nlm.nih.gov/pubmed/14636592 14636592]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qwj ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: N-acylneuraminate cytidylyltransferase]]
[[Category: Gerardy-Schahn R]]
[[Category: Single protein]]
[[Category: Huber R]]
[[Category: Gerardy-Schahn, R.]]
[[Category: Jacob U]]
[[Category: Huber, R.]]
[[Category: Kaiser JT]]
[[Category: Jacob, U.]]
[[Category: Krapp S]]
[[Category: Kaiser, J T.]]
[[Category: Muenster-Kuehnel AK]]
[[Category: Krapp, S.]]
[[Category: Tiralongo J]]
[[Category: Muenster-Kuehnel, A K.]]
[[Category: Tiralongo, J.]]
[[Category: NCC]]
[[Category: cmp-5-n-acetylneuraminic acid synthetase]]
[[Category: cmp-neu5ac]]
[[Category: glycosylation]]
[[Category: lipopolysaccharide biosynthesis]]
[[Category: sialic acid]]
[[Category: sugar-activating enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:37 2008''

Latest revision as of 08:18, 14 February 2024

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

1qwj, resolution 2.80Å

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