1kws

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==Overview==
==Overview==
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Beta1,3-glucuronyltransferase (GlcAT-I) is an essential enzyme involved in, heparan sulfate and chondroitin sulfate biosynthesis. GlcAT-I is an, inverting glycosyltransferase that catalyzes the transfer of glucuronic, acid (GlcUA) to the common growing linker region Galbeta1-3Galbeta1-4Xyl, that is attached to a serine side chain of a core protein. Previously the, structure of GlcAT-I has been solved in the presence of the donor product, UDP and an acceptor analog Galbeta1-3Galbeta1-4Xyl (Pedersen, L. C., Tsuchida, K., Kitagawa, H., Sugahara, K., Darden, T. A. & Negishi, M., (2000) J. Biol. Chem. 275, 34580-34585). Here we report the x-ray crystal, structure of GlcAT-I in complex with the complete donor UDP-GlcUA, thereby, providing structures of an inverting glycosyltransferase in which both the, complete donor and acceptor substrates are present in the active site., This structure supports the in-line displacement reaction mechanism, previously proposed. It also provides information on the essential amino, acid residues that determine donor substrate specificity.
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Beta1,3-glucuronyltransferase (GlcAT-I) is an essential enzyme involved in heparan sulfate and chondroitin sulfate biosynthesis. GlcAT-I is an inverting glycosyltransferase that catalyzes the transfer of glucuronic acid (GlcUA) to the common growing linker region Galbeta1-3Galbeta1-4Xyl that is attached to a serine side chain of a core protein. Previously the structure of GlcAT-I has been solved in the presence of the donor product UDP and an acceptor analog Galbeta1-3Galbeta1-4Xyl (Pedersen, L. C., Tsuchida, K., Kitagawa, H., Sugahara, K., Darden, T. A. & Negishi, M. (2000) J. Biol. Chem. 275, 34580-34585). Here we report the x-ray crystal structure of GlcAT-I in complex with the complete donor UDP-GlcUA, thereby providing structures of an inverting glycosyltransferase in which both the complete donor and acceptor substrates are present in the active site. This structure supports the in-line displacement reaction mechanism previously proposed. It also provides information on the essential amino acid residues that determine donor substrate specificity.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Darden, T.A.]]
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[[Category: Darden, T A.]]
[[Category: Negishi, M.]]
[[Category: Negishi, M.]]
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[[Category: Pedersen, L.C.]]
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[[Category: Pedersen, L C.]]
[[Category: MN]]
[[Category: MN]]
[[Category: UGA]]
[[Category: UGA]]
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[[Category: ntp binding domain]]
[[Category: ntp binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:46 2008''

Revision as of 11:38, 21 February 2008


1kws, resolution 2.10Å

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CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR

Overview

Beta1,3-glucuronyltransferase (GlcAT-I) is an essential enzyme involved in heparan sulfate and chondroitin sulfate biosynthesis. GlcAT-I is an inverting glycosyltransferase that catalyzes the transfer of glucuronic acid (GlcUA) to the common growing linker region Galbeta1-3Galbeta1-4Xyl that is attached to a serine side chain of a core protein. Previously the structure of GlcAT-I has been solved in the presence of the donor product UDP and an acceptor analog Galbeta1-3Galbeta1-4Xyl (Pedersen, L. C., Tsuchida, K., Kitagawa, H., Sugahara, K., Darden, T. A. & Negishi, M. (2000) J. Biol. Chem. 275, 34580-34585). Here we report the x-ray crystal structure of GlcAT-I in complex with the complete donor UDP-GlcUA, thereby providing structures of an inverting glycosyltransferase in which both the complete donor and acceptor substrates are present in the active site. This structure supports the in-line displacement reaction mechanism previously proposed. It also provides information on the essential amino acid residues that determine donor substrate specificity.

About this Structure

1KWS is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA., Pedersen LC, Darden TA, Negishi M, J Biol Chem. 2002 Jun 14;277(24):21869-73. Epub 2002 Apr 11. PMID:11950836

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