2d0j: Difference between revisions

<table><tr><td colspan='2'>[[2d0j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D0J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D0J FirstGlance]. <br>

</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&#8491;</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=2d0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d0j OCA], [https://pdbe.org/2d0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d0j RCSB], [https://www.ebi.ac.uk/pdbsum/2d0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d0j ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/B3GA2_HUMAN B3GA2_HUMAN] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins (By similarity).

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/2d0j_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</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=2d0j ConSurf].

The HNK-1 carbohydrate epitope is found in various neural cell adhesion molecules. Two glucuronyltransferases (GlcAT-P and GlcAT-S) are involved in the biosynthesis of HNK-1 carbohydrate. Our previous study on the crystal structure of GlcAT-P revealed the reaction and substrate recognition mechanisms of this enzyme. Comparative analyses of the enzymatic activities of GlcAT-S and GlcAT-P showed that there are notable differences in the acceptor substrate specificities of these enzymes. To elucidate differences between their specificities, we now solved the crystal structure of GlcAT-S. Residues interacting with UDP molecule, which is a part of the donor substrate, are highly conserved between GlcAT-P and GlcAT-S. On the other hand, there are some differences between these proteins in the manner they recognize their respective acceptor substrates. Phe245, one of the most important GlcAT-P residues for the recognition of acceptors, is a tryptophan in GlcAT-S. In addition, Val320, which is located on the C-terminal long loop of the neighboring molecule in the dimer and critical in the recognition of the acceptor sugar molecule by the GlcAT-P dimer, is an alanine in GlcAT-S. These differences play key roles in establishing the distinct specificity for the acceptor substrate by GlcAT-S, which is further supported by site-directed mutagenesis of GlcAT-S and a computer-aided model building of GlcAT-S/substrate complexes.

Crystal structure of GlcAT-S, a human glucuronyltransferase, involved in the biosynthesis of the HNK-1 carbohydrate epitope.,Shiba T, Kakuda S, Ishiguro M, Morita I, Oka S, Kawasaki T, Wakatsuki S, Kato R Proteins. 2006 Nov 1;65(2):499-508. PMID:16897771<ref>PMID:16897771</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 2d0j" style="background-color:#fffaf0;"></div>

== References ==

[[Category: Ishiguro M]]

[[Category: Kakuda S]]

[[Category: Kato R]]

[[Category: Kawasaki T]]

[[Category: Oka S]]

[[Category: Shiba T]]

[[Category: Wakatsuki S]]