1gx0

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[[Image:1gx0.gif|left|200px]]<br />
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[[Image:1gx0.gif|left|200px]]<br /><applet load="1gx0" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1gx0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1gx0, resolution 1.80&Aring;" />
caption="1gx0, resolution 1.80&Aring;" />
'''ALPHA-,1,3 GALACTOSYLTRANSFERASE- BETA-D-GALACTOSE COMPLEX'''<br />
'''ALPHA-,1,3 GALACTOSYLTRANSFERASE- BETA-D-GALACTOSE COMPLEX'''<br />
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==About this Structure==
==About this Structure==
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1GX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GAL, MN, UDP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.4.1.87 Transferred entry: 2.4.1.87], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.151 2.4.1.151] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GX0 OCA].
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1GX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GAL, MN, UDP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.4.1.87 Transferred entry: 2.4.1.87], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.151 2.4.1.151] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GX0 OCA].
==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:21:55 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:43:45 2007''

Revision as of 13:33, 18 December 2007


1gx0, resolution 1.80Å

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ALPHA-,1,3 GALACTOSYLTRANSFERASE- BETA-D-GALACTOSE COMPLEX

Overview

Bovine alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the synthesis, of the alpha-galactose (alpha-Gal) epitope, the target of natural human, antibodies. It represents a family of enzymes, including the histo blood, group A and B transferases, that catalyze retaining glycosyltransfer, reactions of unknown mechanism. An initial study of alpha3GT in a crystal, form with limited resolution and considerable disorder suggested the, possible formation of a beta-galactosyl-enzyme covalent intermediate, (Gastinel, L. N., Bignon, C., Misra, A. K., Hindsgaul, O., Shaper, J. H., and Joziasse, D. H. (2001) EMBO J. 20, 638-649). Highly ordered structures, are described for complexes of alpha3GT with donor substrate, UDP-galactose, UDP- glucose, and two acceptor substrates, lactose and, N-acetyllactosamine, at resolutions up to 1.46 A. Structural and, calorimetric binding studies suggest an obligatory ordered binding of, donor and acceptor substrates, linked to a donor substrate-induced, conformational change, and the direct participation of UDP in acceptor, binding. The monosaccharide-UDP bond is cleaved in the structures, containing UDP-galactose and UDP-glucose, producing non-covalent complexes, containing buried beta-galactose and alpha-glucose. The location of these, monosaccharides and molecular modeling suggest that binding of a distorted, conformation of UDP-galactose may be important in the catalytic mechanism, of alpha3GT.

About this Structure

1GX0 is a Single protein structure of sequence from Bos taurus with GAL, MN, UDP and GOL as ligands. Active as Transferred entry: 2.4.1.87, with EC number 2.4.1.151 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase., Boix E, Zhang Y, Swaminathan GJ, Brew K, Acharya KR, J Biol Chem. 2002 Aug 2;277(31):28310-8. Epub 2002 May 14. PMID:12011052

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