View source for 2jzc


==NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1==
<StructureSection load='2jzc' size='340' side='right'caption='[[2jzc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jzc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JZC 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=2jzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzc OCA], [https://pdbe.org/2jzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jzc RCSB], [https://www.ebi.ac.uk/pdbsum/2jzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzc ProSAT], [https://www.topsan.org/Proteins/NESGC/2jzc TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALG13_YEAST ALG13_YEAST] Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.<ref>PMID:15615718</ref> <ref>PMID:16100110</ref> 
== 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/jz/2jzc_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=2jzc ConSurf].
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== Publication Abstract from PubMed ==
The solution structure of Alg13, the glycosyl donor-binding domain of an important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae, is presented. This glycosyltransferase is unusual in that it is active only in the presence of a binding partner, Alg14. Alg13 is found to adopt a unique topology among glycosyltransferases. Rather than the conventional Rossmann fold found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the C-terminal half of Alg13 is conserved. However, although conventional GT-B enzymes usually possess three helices at the C terminus, only two helices are present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13 with the sugar donor is primarily through the residues in the C-terminal half of the protein.

Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.,Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH Structure. 2008 Jun;16(6):965-75. PMID:18547528<ref>PMID:18547528</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jzc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Imepriali B]]
[[Category: Montelione GT]]
[[Category: Prestegard JH]]
[[Category: Wang X]]
[[Category: Weldeghorghis T]]
[[Category: Zhang G]]