4M98
Acetyltransferase domain of PglB from Neisseria gonorrhoeae FA1090
Summary for 4M98
| Entry DOI | 10.2210/pdb4m98/pdb |
| Related | 4M99 4M9C |
| Descriptor | Pilin glycosylation protein (2 entities in total) |
| Functional Keywords | left-handed beta-helix, rossmann fold, acetyltransferase, transferase |
| Biological source | Neisseria gonorrhoeae |
| Total number of polymer chains | 1 |
| Total formula weight | 21032.94 |
| Authors | Morrison, M.J.,Imperiali, B. (deposition date: 2013-08-14, release date: 2013-10-02, Last modification date: 2023-09-20) |
| Primary citation | Morrison, M.J.,Imperiali, B. Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine. J.Biol.Chem., 288:32248-32260, 2013 Cited by PubMed Abstract: 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 β-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. PubMed: 24064219DOI: 10.1074/jbc.M113.510560 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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