1fgg: Difference between revisions

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[[Image:1fgg.gif|left|200px]]
{{Seed}}
[[Image:1fgg.png|left|200px]]


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{{STRUCTURE_1fgg|  PDB=1fgg  |  SCENE=  }}  
{{STRUCTURE_1fgg|  PDB=1fgg  |  SCENE=  }}  


'''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+===




==Overview==
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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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{{ABSTRACT_PUBMED_10946001}}


==About this Structure==
==About this Structure==
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[[Category: Glucuronyltransferase]]
[[Category: Glucuronyltransferase]]
[[Category: Udp]]
[[Category: Udp]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:17:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:12:42 2008''

Revision as of 00:12, 1 July 2008

File:1fgg.png

Template:STRUCTURE 1fgg

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

Template:ABSTRACT PUBMED 10946001

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

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