Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers
Harrus, Deborah; Kellokumpu, Sakari; Glumoff, Tuomo (2017-09-20)
Harrus, D., Kellokumpu, S. & Glumoff, T. Cell. Mol. Life Sci. (2018) 75: 833. https://doi.org/10.1007/s00018-017-2659-x
© Springer International Publishing AG 2017. This is a post-peer-review, pre-copyedit version of an article published in Cellular and molecular life sciences. The final authenticated version is available online at: http://dx.doi.org/10.1007/s00018-017-2659-x.
Glycosyltransferases (GTases) transfer sugar moieties to proteins, lipids or existing glycan or polysaccharide molecules. GTases form an important group of enzymes in the Golgi, where the synthesis and modification of glycoproteins and glycolipids take place. Golgi GTases are almost invariably type II integral membrane proteins, with the C-terminal globular catalytic domain residing in the Golgi lumen. The enzymes themselves are divided into 103 families based on their sequence homology. There is an abundance of published crystal structures of GTase catalytic domains deposited in the Protein Data Bank (PDB). All of these represent either of the two main characteristic structural folds, GT-A or GT-B, or present a variation thereof. Since GTases can function as homomeric or heteromeric complexes in vivo, we have summarized the structural features of the dimerization interfaces in crystal structures of GTases, as well as considered the biochemical data available for these enzymes. For this review, we have considered all 898 GTase crystal structures in the Protein Data Bank and highlight the dimer formation characteristics of various GTases based on 24 selected structures.
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