1kws: Difference between revisions

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==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.

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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Darden, T.A.]]

[[Category: Darden, T A.]]

[[Category: Negishi, M.]]

[[Category: Pedersen, L.C.]]

[[Category: Pedersen, L C.]]

[[Category: MN]]

[[Category: UGA]]

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[[Category: ntp binding domain]]

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@@ Line 4: / Line 4: @@
 ==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. &amp; 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.
+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. &amp; 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==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Darden, T.A.]]
+[[Category: Darden, T A.]]
 [[Category: Negishi, M.]]
-[[Category: Pedersen, L.C.]]
+[[Category: Pedersen, L C.]]
 [[Category: MN]]
 [[Category: UGA]]
@@ Line 21: / Line 21: @@
 [[Category: ntp binding domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:46 2008''