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3ewi

From Proteopedia

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{{Seed}}
 
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[[Image:3ewi.jpg|left|200px]]
 
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==Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase==
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The line below this paragraph, containing "STRUCTURE_3ewi", creates the "Structure Box" on the page.
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<StructureSection load='3ewi' size='340' side='right'caption='[[3ewi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ewi]] is a 2 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=3EWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EWI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ewi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ewi OCA], [https://pdbe.org/3ewi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ewi RCSB], [https://www.ebi.ac.uk/pdbsum/3ewi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ewi ProSAT]</span></td></tr>
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{{STRUCTURE_3ewi| PDB=3ewi | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ew/3ewi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3ewi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The biosynthesis of sialic acid-containing glycoconjugates is crucial for the development of vertebrate life. Cytidine monophosphate-sialic acid synthetase (CSS) catalyzes the metabolic activation of sialic acids. In vertebrates, the enzyme is chimeric, with the N-terminal domain harboring the synthetase activity. The function of the highly conserved C-terminal domain (CSS-CT) is unknown. To shed light on its biological function, we solved the X-ray structure of murine CSS-CT to 1.9 A resolution. CSS-CT is a stable shamrock-like tetramer that superimposes well with phosphatases of the haloacid dehalogenase superfamily. However, a region found exclusively in vertebrate CSS-CT appears to block the active-site entrance. Accordingly, no phosphatase activity was observed in vitro, which points toward a nonenzymatic function of CSS-CT. A computational three-dimensional model of full-length CSS, in combination with in vitro oligomerization studies, provides evidence that CSS-CT serves as a platform for the quaternary organization governing the kinetic properties of the physiologically active enzyme as demonstrated in kinetic studies.
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===Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase===
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A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme.,Oschlies M, Dickmanns A, Haselhorst T, Schaper W, Stummeyer K, Tiralongo J, Weinhold B, Gerardy-Schahn R, von Itzstein M, Ficner R, Munster-Kuhnel AK J Mol Biol. 2009 Oct 16;393(1):83-97. Epub 2009 Aug 8. PMID:19666032<ref>PMID:19666032</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<!--
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19666032}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3ewi" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19666032 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19666032}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3EWI is a 2 chains structure of sequences 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=3EWI OCA].
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==Reference==
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<ref group="xtra">PMID:19666032</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: N-acylneuraminate cytidylyltransferase]]
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[[Category: Dickmanns A]]
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[[Category: Dickmanns, A.]]
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[[Category: Ficner R]]
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[[Category: Ficner, R.]]
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[[Category: Gerardy-Schahn R]]
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[[Category: Gerardy-Schahn, R.]]
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[[Category: Muenster-Kuehnel AK]]
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[[Category: Muenster-Kuehnel, A K.]]
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[[Category: Oschlies M]]
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[[Category: Oschlies, M.]]
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[[Category: Stummeyer K]]
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[[Category: Stummeyer, K.]]
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[[Category: Beta barrel]]
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[[Category: Had-like]]
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[[Category: Nucleotidyltransferase]]
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[[Category: Nucleus]]
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[[Category: Rossmannoid fold]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 19 13:07:23 2009''
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Current revision

Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase

PDB ID 3ewi

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