2d0j

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[[Image:2d0j.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Human GlcAT-S Apo Form==
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|PDB= 2d0j |SIZE=350|CAPTION= <scene name='initialview01'>2d0j</scene>, resolution 2.0&Aring;
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<StructureSection load='2d0j' size='340' side='right'caption='[[2d0j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span>
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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]] 2&#8491;</td></tr>
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|GENE=
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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=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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d0j OCA], [http://www.ebi.ac.uk/pdbsum/2d0j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d0j RCSB]</span>
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[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).
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}}
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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/d0/2d0j_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=2d0j 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 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.
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'''Crystal Structure of Human GlcAT-S Apo Form'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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2D0J is a [[Single protein]] structure of sequence from [http://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].
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<div class="pdbe-citations 2d0j" style="background-color:#fffaf0;"></div>
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[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ishiguro, M.]]
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[[Category: Ishiguro M]]
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[[Category: Kakuda, S.]]
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[[Category: Kakuda S]]
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[[Category: Kato, R.]]
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[[Category: Kato R]]
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[[Category: Kawasaki, T.]]
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[[Category: Kawasaki T]]
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[[Category: Oka, S.]]
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[[Category: Oka S]]
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[[Category: Shiba, T.]]
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[[Category: Shiba T]]
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[[Category: Wakatsuki, S.]]
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[[Category: Wakatsuki S]]
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[[Category: glucuronyltransferase]]
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[[Category: rossmann-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:28:42 2008''
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Current revision

Crystal Structure of Human GlcAT-S Apo Form

PDB ID 2d0j

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