1. Academic Validation
  2. Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen

Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen

  • Sci Rep. 2012;2:940. doi: 10.1038/srep00940.
Nethaji Thiyagarajan 1 Tram T K Pham Brittany Stinson Amit Sundriyal Percy Tumbale Michelle Lizotte-Waniewski Keith Brew K Ravi Acharya
Affiliations

Affiliation

  • 1 Department of Biology and Biochemistry, University of Bath , Claverton Down, Bath BA2 7AY, UK.
Abstract

Histo-blood group antigens (HBGAs) are a source of antigenic variation between individuals that modulates resistance and susceptibility to pathogens and is a barrier to the spread of enveloped viruses. HBGAs are also produced by a few prokaryotes where they are synthesized by glycosyltransferases (GTs) related to human HBGA synthases. Here we report the first structure of a Bacterial GT of this family, from an intestinal resident, Bacteroides ovatus. Unlike its mammalian homologues and Other GTs with similar folds, this protein lacks a metal-binding Asp-X-Asp motif and is fully active in the absence of divalent metal ions, yet is strikingly similar in structure and in its interactions with substrates to structurally characterized mammalian metal-dependent mammalian homologues. This shows how an apparently major divergence in catalytic properties can be accommodated by minor structural adjustments and illustrates the structural underpinnings of horizontal transfer of a functional gene from prokaryotes to vertebrates.

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