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

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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
    Present Address: Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China)

  • 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
    Institute of Oral Health Research, School of Medicine, University of Alabama at Birmingham)

  • Hui Wu

    (Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham)

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.

Suggested Citation

  • Hua Zhang & Fan Zhu & Tiandi Yang & Lei Ding & Meixian Zhou & Jingzhi Li & Stuart M. Haslam & Anne Dell & Heidi Erlandsen & Hui Wu, 2014. "The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold," Nature Communications, Nature, vol. 5(1), pages 1-12, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5339
    DOI: 10.1038/ncomms5339
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