Literature summary for 2.4.1.87 extracted from

Jamaluddin, H.; Tumbale, P.; Withers, S.G.; Acharya, K.R.; Brew, K.
Conformational changes induced by binding UDP-2F-galactose to alpha-1,3galactosyltransferase - implications for catalysis (2007), J. Mol. Biol., 369, 1270-1281.

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo crystals of alpha3GT are grown by the vapour-diffusion, hanging-drop method. Structure of a complex containing an inhibitory analogue of UDP-galactose, UDP-2F-galactose, in a complex with the Arg365Lys mutant of alpha3GT. The binding of a donor substrate analogue induces conformational changes in both the ligand and the enzyme. Two loops of alpha3GT are stabilized in the complex of which the C-terminal region, in particular, is highly flexible. Structural transitions in this region are connected with donor substrate binding and distortion (ground state destabilization), cleavage of the UDP to galactose bond, formation of a binding site for acceptor substrate and UDP release	Bos taurus

Crystallization (Comment)

Organism

apo crystals of alpha3GT are grown by the vapour-diffusion, hanging-drop method. Structure of a complex containing an inhibitory analogue of UDP-galactose, UDP-2F-galactose, in a complex with the Arg365Lys mutant of alpha3GT. The binding of a donor substrate analogue induces conformational changes in both the ligand and the enzyme. Two loops of alpha3GT are stabilized in the complex of which the C-terminal region, in particular, is highly flexible. Structural transitions in this region are connected with donor substrate binding and distortion (ground state destabilization), cleavage of the UDP to galactose bond, formation of a binding site for acceptor substrate and UDP release

Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P14769	recombinantly expressed in Escherichia coli	-

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Release 2023.1 (January 2023)