The Conformational Plasticity of Glycosyl Transferases
Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from nucleotide-sugar or lipid-phospho-sugar donors to a broad range of acceptor substrates, generating a significant amount of structural diversity in biological systems. GTs are highly selective in nature, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their sugar and acceptor substrates.
The article summarizes key points which have been characterized over the recent years enlightening how GTs have gained functionality and diversity throughout undergoing a series of mechanisms where structural plasticity played a major role. The nature of the catalytic mechanisms of ‘inverting’ and ‘retaining’ GTs has been more precisely established throughout 3 dimensional structures and theoretical approaches. Yet, the mode of action of these enzymes remains to be determined in regards to the interplay of the substrate/membrane associations where not only the structure of proteins but their dynamics play a determinant role.