4AYJ
Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen
Summary for 4AYJ
| Entry DOI | 10.2210/pdb4ayj/pdb |
| Related | 4AYL |
| Related PRD ID | PRD_900070 |
| Descriptor | BOGT - METAL-INDEPENDENT GLYCOSYLTRANSFERASE, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | transferase, catalysis |
| Biological source | BACTEROIDES OVATUS |
| Total number of polymer chains | 4 |
| Total formula weight | 118105.98 |
| Authors | Thiyagarajan, N.,Pham, T.T.K.,Stinson, B.,Sundriyal, A.,Tumbale, P.,Lizotte-Waniewskib, M.,Brewb, K.,Acharya, K.R. (deposition date: 2012-06-21, release date: 2012-12-19, Last modification date: 2023-12-20) |
| Primary citation | Thiyagarajan, N.,Pham, T.T.K.,Stinson, B.,Sundriyal, A.,Tumbale, P.,Lizotte-Waniewski, M.,Brew, K.,Acharya, K.R. Structure of a Metal-Independent Bacterial Glycosyltransferase that Catalyzes the Synthesis of Histo-Blood Group a Antigen Sci.Rep., 2:940-, 2012 Cited by PubMed 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. PubMed: 23230506DOI: 10.1038/SREP00940 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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