1fgg
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fgg |SIZE=350|CAPTION= <scene name='initialview01'>1fgg</scene>, resolution 2.30Å | |PDB= 1fgg |SIZE=350|CAPTION= <scene name='initialview01'>1fgg</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> | + | |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'-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Sugahara, K.]] | [[Category: Sugahara, K.]] | ||
[[Category: Tsuchida, K]] | [[Category: Tsuchida, K]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: UDP]] | ||
| - | [[Category: UNX]] | ||
[[Category: ddd]] | [[Category: ddd]] | ||
[[Category: glucuronyltransferase]] | [[Category: glucuronyltransferase]] | ||
[[Category: udp]] | [[Category: udp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:22:23 2008'' |
Revision as of 17:22, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:22:23 2008
