View source for 1wvo


==Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.==
<StructureSection load='1wvo' size='340' side='right'caption='[[1wvo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wvo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvo OCA], [https://pdbe.org/1wvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvo RCSB], [https://www.ebi.ac.uk/pdbsum/1wvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvo ProSAT], [https://www.topsan.org/Proteins/RSGI/1wvo TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SIAS_HUMAN SIAS_HUMAN] Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/1wvo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wvo ConSurf].
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== Publication Abstract from PubMed ==
The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface.

Solution structure of the antifreeze-like domain of human sialic acid synthase.,Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820<ref>PMID:16597820</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hamada T]]
[[Category: Hayashi F]]
[[Category: Hirota H]]
[[Category: Ito Y]]
[[Category: Yokoyama S]]