University of Oulu

Harrus, D., Kellokumpu, S. & Glumoff, T. Cell. Mol. Life Sci. (2018) 75: 833.

Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers

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Author: Harrus, Deborah1; Kellokumpu, Sakari1; Glumoff, Tuomo1
Organizations: 1Faculty of Biochemistry and Molecular Medicine, University of Oulu, PO Box 5400, 90014 Oulu, Finland
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 5.9 MB)
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Language: English
Published: Springer Nature, 2017
Publish Date: 2018-09-20


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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Series: Cellular and molecular life sciences
ISSN: 1420-682X
ISSN-E: 1420-9071
ISSN-L: 1420-682X
Volume: 75
Issue: 5
Pages: 833 - 848
DOI: 10.1007/s00018-017-2659-x
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: The financial support from the Academy of Finland (no. 285232, date 11.05.2015), University of Oulu, and Emil Aaltonen Foundation is gratefully acknowledged.
Academy of Finland Grant Number: 285232
Detailed Information: 285232 (Academy of Finland Funding decision)
Copyright information: © 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: