1fgg

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[[Image:1fgg.gif|left|200px]]
[[Image:1fgg.gif|left|200px]]
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{{Structure
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|PDB= 1fgg |SIZE=350|CAPTION= <scene name='initialview01'>1fgg</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1fgg", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5&#39;-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>
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{{STRUCTURE_1fgg| PDB=1fgg | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgg OCA], [http://www.ebi.ac.uk/pdbsum/1fgg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fgg RCSB]</span>
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'''CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+'''
'''CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+'''
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[[Category: Sugahara, K.]]
[[Category: Sugahara, K.]]
[[Category: Tsuchida, K]]
[[Category: Tsuchida, K]]
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[[Category: ddd]]
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[[Category: Ddd]]
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[[Category: glucuronyltransferase]]
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[[Category: Glucuronyltransferase]]
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[[Category: udp]]
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[[Category: Udp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:17:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:22:23 2008''
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Revision as of 13:17, 2 May 2008

Image:1fgg.gif

Template:STRUCTURE 1fgg

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


Overview

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.

About this Structure

1FGG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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:10946001 Page seeded by OCA on Fri May 2 16:17:49 2008

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