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1gww

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[[Category: transferase]]
[[Category: transferase]]
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Revision as of 14:16, 5 November 2007


1gww, resolution 1.80Å

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ALPHA-,1,3 GALACTOSYLTRANSFERASE- ALPHA-D-GLUCOSE 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

1GWW is a Single protein structure of sequence from Bos taurus with GLC, MN and UDP as ligands. Active as Transferred entry: 2.4.1.87, with EC number 2.4.1.151 Structure known Active Site: AC1. 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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