4AYL: Molecular Structure Of A Metal-independent Bacterial Glycosyltransferase That Catalyzes The Synthesis Of Histo- Blood Group A Antigen

Citation:
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.
PDB ID: 4AYLDownload
MMDB ID: 105903
PDB Deposition Date: 2012/6/21
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.92  Å
Source Organism:
Similar Structures:
Biological Unit for 4AYL: monomeric; determined by author and by software (PISA)
Molecular Components in 4AYL
Label Count Molecule
Protein (1 molecule)
1
Bogt-metal-independent Glycosyltransferase
Molecule annotation
Chemicals (3 molecules)
1
1
2
1
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.