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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11: XN4Q5

]

NCBI PubMed ID: 24064219
Publication DOI: 10.1074/jbc.M113.510560
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: B. Imperiali <imper

mit.edu>
Institutions: From the Departments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac) is a unique carbohydrate produced by a number of bacterial species and has been implicated in pathogenesis. The terminal step in the formation of this important bacterial sugar is catalyzed by an acetyl-CoA (AcCoA)-dependent acetyltransferase in both N- and O-linked protein glycosylation pathways. This bacterial acetyltransferase is a member of the left-handed beta-helix family and forms a homotrimer as the functional unit. Whereas previous endeavors have focused on the Campylobacter jejuni acetyltransferase (PglD) from the N-linked glycosylation pathway, structural characterization of the homologous enzymes in the O-linked glycosylation pathways is lacking. Herein, we present the apo-crystal structures of the acetyltransferase domain (ATD) from the bifunctional enzyme PglB (Neisseria gonorrhoeae) and the full-length acetyltransferase WeeI (Acinetobacter baumannii). Additionally, a PglB-ATD structure was solved in complex with AcCoA. Surprisingly, this structure reveals a contrasting binding mechanism for this substrate when compared with the AcCoA-bound PglD structure. A comparison between these findings and the previously solved PglD crystal structures illustrates a dichotomy among N- and O-linked glycosylation pathway enzymes. Based upon these structures, key residues in the UDP-4-amino and AcCoA binding pockets were mutated to determine their effect on binding and catalysis in PglD, PglB-ATD, and WeeI. Last, a phylogenetic analysis of the aforementioned acetyltransferases was employed to illuminate the diversity among N- and O-linked glycosylation pathway enzymes.

biosynthesis, structure, Acinetobacter, Campylobacter jejuni, Gonorrhoeae, Neisseria gonorrhoeae, glycosylation, N-linked, O-linked, acetyltransferases

Structure type: oligomer
Location inside paper: p.32248, fig.1
Aglycon: peptide
Compound class: N-glycan
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_885822,IEDB_983931,SB_192

Methods: SDS-PAGE, genetic methods, biochemical methods, crystallization
3D data: 3D data

Related record ID(s): 29654
NCBI Taxonomy refs (TaxIDs): 197
Reference(s) to other database(s): GTC:G58528CE
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1[C@@H](O)O[C@H](C)[C@@H](NC(C)=O)[C@@H]1O[C@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)[C@H](O[C@H]3O[C@H](CO)[C@H](O[C@H]4O[C@H](CO)[C@H](O[C@H]5O[C@H](CO)[C@H](O)[C@H](O)[C@H]5NC(C)=O)[C@H](O)[C@H]4NC(C)=O)[C@H](O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)[C@H]3NC(C)=O)[C@H](O)[C@H]2NC(C)=O)[C@H](O)[C@H]1NC(C)=O

SVG MW SMILES 3D mol Ionize