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1fgg

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(New page: 200px<br /> <applet load="1fgg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgg, resolution 2.30&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1fgg.gif|left|200px]]<br />
 
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<applet load="1fgg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fgg, resolution 2.30&Aring;" />
 
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'''CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+==
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Human beta1,3-glucuronyltransferase I (GlcAT-I) is a central enzyme in the, initial steps of proteoglycan synthesis. GlcAT-I transfers a glucuronic, acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to, the common linkage region trisaccharide Gal beta 1-3Gal beta 1-4Xyl, covalently bound to a Ser residue at the glycosaminylglycan attachment, site of proteoglycans. We have now determined the crystal structure of, GlcAT-1 at 2.3 A in the presence of the donor substrate product UDP, the, catalytic Mn(2+) ion, and the acceptor substrate analog Gal beta 1-3Gal, beta 1-4Xyl. The enzyme is a alpha/beta protein with two subdomains that, constitute the donor and acceptor substrate binding site. The active site, residues lie in a cleft extending across both subdomains in which the, trisaccharide molecule is oriented perpendicular to the UDP. Residues, Glu(227), Asp(252), and Glu(281) dictate the binding orientation of the, terminal Gal-2 moiety. Residue Glu(281) is in position to function as a, catalytic base by deprotonating the incoming 3-hydroxyl group of the, acceptor. The conserved DXD motif (Asp(194), Asp(195), Asp(196)) has, direct interaction with the ribose of the UDP molecule as well as with the, Mn(2+) ion. The key residues involved in substrate binding and catalysis, are conserved in the glucuronyltransferase family as well as other, glycosyltransferases.
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<StructureSection load='1fgg' size='340' side='right'caption='[[1fgg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fgg]] is a 2 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=1FGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGG FirstGlance]. <br>
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1FGG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN, UDP and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGG OCA].
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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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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==Reference==
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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=1fgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgg OCA], [https://pdbe.org/1fgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgg RCSB], [https://www.ebi.ac.uk/pdbsum/1fgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgg ProSAT]</span></td></tr>
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Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I., Pedersen LC, Tsuchida K, Kitagawa H, Sugahara K, Darden TA, Negishi M, J Biol Chem. 2000 Nov 3;275(44):34580-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10946001 10946001]
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/B3GA3_HUMAN B3GA3_HUMAN] Defects in B3GAT3 are the cause of multiple joint dislocations short stature craniofacial dysmorphism and congenital heart defects (JDSSDHD) [MIM:[https://omim.org/entry/245600 245600]. An autosomal recessive disease characterized by dysmorphic facies, bilateral dislocations of the elbows, hips, and knees, clubfeet, and short stature, as well as cardiovascular defects.<ref>PMID:21763480</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/B3GA3_HUMAN B3GA3_HUMAN] Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.
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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/fg/1fgg_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=1fgg ConSurf].
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<div style="clear:both"></div>
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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: Darden, T.A.]]
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[[Category: Darden TA]]
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[[Category: Kitagawa, H.]]
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[[Category: Kitagawa H]]
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[[Category: Pedersen, L.C.]]
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[[Category: Pedersen LC]]
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[[Category: Sugahara, K.]]
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[[Category: Sugahara K]]
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[[Category: Tsuchida, K]]
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[[Category: Tsuchida K]]
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[[Category: MN]]
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[[Category: UDP]]
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[[Category: UNX]]
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[[Category: ddd]]
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[[Category: glucuronyltransferase]]
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[[Category: udp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:52:56 2007''
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Current revision

CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+

PDB ID 1fgg

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