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Curr Opin Struct Biol. 2004 Oct;14(5):593-600.

Structure and catalytic cycle of beta-1,4-galactosyltransferase.

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Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, Center for Cancer Research, NCI-Frederick, MD 21702, USA.


Beta-1,4-galactosyltransferase-1, a housekeeping enzyme that functions in the synthesis of glycoconjugates, has two flexible loops, one short and one long. Upon binding a metal ion and UDP-galactose, the loops change from an open to a closed conformation, repositioning residues to lock the ligands in place. Residues at the N-terminal region of the long loop form the metal-binding site and those at the C-terminal region form a helix, which becomes part of the binding site for the oligosaccharide acceptor; the remaining residues cover the bound sugar-nucleotide. After binding of the oligosaccharide acceptor and transfer of the galactose moiety, the product disaccharide unit is ejected and the enzyme returns to the open conformation, repeating the catalytic cycle.

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