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Nat Commun. 2014 Jul 15;5:4339. doi: 10.1038/ncomms5339.

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

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  • 1Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
  • 2Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
  • 3Department of Biochemistry and Molecular Genetics, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
  • 41] Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA [2].
  • 5Department of Cell Biology, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
  • 61] Department of Periodontology, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA [2] Institute of Oral Health Research, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.

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.

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