The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold

Hua Zhang, Fan Zhu, Tiandi Yang, Lei Ding, Meixian Zhou, Jingzhi Li, Stuart M. Haslam, Anne Dell, Heidi Erlandsen and Hui Wu ()
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Hua Zhang: Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham
Fan Zhu: Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham
Tiandi Yang: Imperial College London
Lei Ding: School of Medicine, University of Alabama at Birmingham
Meixian Zhou: Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham
Jingzhi Li: School of Medicine, University of Alabama at Birmingham
Stuart M. Haslam: Imperial College London
Anne Dell: Imperial College London
Heidi Erlandsen: School of Medicine, University of Alabama at Birmingham
Hui Wu: Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract More than 33,000 glycosyltransferases have been identified. Structural studies, however, have only revealed two distinct glycosyltransferase (GT) folds, GT-A and GT-B. Here we report a 1.34-Å resolution X-ray crystallographic structure of a previously uncharacterized ‘domain of unknown function’ 1792 (DUF1792) and show that the domain adopts a new fold and is required for glycosylation of a family of serine-rich repeat streptococcal adhesins. Biochemical studies reveal that the domain is a glucosyltransferase, and it catalyses the transfer of glucose to the branch point of the hexasaccharide O-linked to the serine-rich repeat of the bacterial adhesin, Fap1 of Streptococcus parasanguinis. DUF1792 homologues from both Gram-positive and Gram-negative bacteria also exhibit the activity. Thus, DUF1792 represents a new family of glycosyltransferases; therefore, we designate it as a GT-D glycosyltransferase fold. As the domain is highly conserved in bacteria and not found in eukaryotes, it can be explored as a new antibacterial target.

Date: 2014
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DOI: 10.1038/ncomms5339

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