4M98

Acetyltransferase domain of PglB from Neisseria gonorrhoeae FA1090

4M98 の概要

• エントリーDOI: 10.2210/pdb4m98/pdb
• 関連するPDBエントリー: 4M99 4M9C
• 分子名称: Pilin glycosylation protein (2 entities in total)
• 機能のキーワード: left-handed beta-helix, rossmann fold, acetyltransferase, transferase
• 由来する生物種: Neisseria gonorrhoeae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21032.94

構造登録者

Morrison, M.J.,Imperiali, B. (登録日: 2013-08-14, 公開日: 2013-10-02, 最終更新日: 2023-09-20)

主引用文献

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

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: 24064219
DOI: 10.1074/jbc.M113.510560

実験手法

X-RAY DIFFRACTION (1.67 Å)