title: The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold.
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.
authors.affiliation: Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Hua
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Fan
authors.initials: F
authors.lastname: Zhu
authors.affiliation: Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
authors.forename: Tiandi
authors.initials: T
authors.lastname: Yang
authors.affiliation: Department of Biochemistry and Molecular Genetics, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Lei
authors.initials: L
authors.lastname: Ding
authors.affiliation: 1] Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA [2].
authors.forename: Meixian
authors.initials: M
authors.lastname: Zhou
authors.affiliation: Department of Cell Biology, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Jingzhi
authors.initials: J
authors.lastname: Li
authors.affiliation: Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Haslam
authors.affiliation: Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
authors.affiliation: 1] 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.
authors.forename: Heidi
authors.initials: H
authors.lastname: Erlandsen
authors.affiliation: Departments of Pediatric Dentistry, Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Hui
authors.initials: H
authors.lastname: Wu
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D015964:Gene Expression Regulation, Bacterial; D016695:Glycosyltransferases / Q000737:chemistry* / Q000378:metabolism*; D013291:Streptococcus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D016695:Glycosyltransferases