Imperial College London
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ProfessorAnneDell

Faculty of Natural Sciences, Department of Life Sciences

Professor of Carbohydrate Bichemistry
 
 
 
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a.dell

 
 
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Location

 

101BSir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Zhang:2016:10.1074/jbc.M116.731695,
author = {Zhang, H and Zhou, M and Yang, T and Haslam, SM and Dell, A and Wu, H},
doi = {10.1074/jbc.M116.731695},
journal = {Journal of Biological Chemistry},
pages = {22106--22117},
title = {A New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional Protein},
url = {http://dx.doi.org/10.1074/jbc.M116.731695},
volume = {291},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Serine-rich repeat glycoproteins (SRRPs) conserved in streptococci and staphylococci are important for bacterial colonization and pathogenesis. Fap1, a well studied SRRP is a major surface constituent of Streptococcus parasanguinis and is required for bacterial adhesion and biofilm formation. Biogenesis of Fap1 is a multistep process that involves both glycosylation and secretion. A series of glycosyltransferases catalyze sequential glycosylation of Fap1. We have identified a unique hybrid protein dGT1 (dual glycosyltransferase 1) that contains two distinct domains. N-terminal DUF1792 is a novel GT-D-type glycosyltransferase, transferring Glc residues to Glc-GlcNAc-modified Fap1. C-terminal dGT1 (CgT) is predicted to possess a typical GT-A-type glycosyltransferase, however, the activity remains unknown. In this study, we determine that CgT is a distinct glycosyltransferase, transferring GlcNAc residues to Glc-Glc-GlcNAc-modified Fap1. A 2.4-Å x-ray crystal structure reveals that CgT has a unique binding domain consisting of three α helices in addition to a typical GT-A-type glycosyltransferase domain. The helical domain is crucial for the oligomerization of CgT. Structural and biochemical studies revealed that the helix domain is required for the protein-protein interaction and crucial for the glycosyltransferase activity of CgT in vitro and in vivo. As the helix domain presents a novel structural fold, we conclude that CgT represents a new member of GT-A-type glycosyltransferases.
AU  - Zhang,H
AU  - Zhou,M
AU  - Yang,T
AU  - Haslam,SM
AU  - Dell,A
AU  - Wu,H
DO  - 10.1074/jbc.M116.731695
EP  - 22117
PY  - 2016///
SN  - 1083-351X
SP  - 22106
TI  - A New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional Protein
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M116.731695
UR  - http://hdl.handle.net/10044/1/39557
VL  - 291
ER  -
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