7S44

Crystal structure of an N-acetyltransferase, C80T mutant, from Helicobacter pullorum in the presence of Coenzyme A and dTDP-3-amino-3,6-dideoxy-D-galactose

7S44 の概要

• エントリーDOI: 10.2210/pdb7s44/pdb
• 関連するPDBエントリー: 7s3u 7s3w 7s41 7s42 7s43
• 分子名称: N-acetyltransferase, (3R,4S,5R,6R)-4-amino-3,5-dihydroxy-6-methyloxan-2-yl][hydroxy-[[(2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy]phosphoryl] hydrogen phosphate, OXIDIZED COENZYME A, ... (6 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Helicobacter pullorum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19692.79

構造登録者

Griffiths, W.A.,Spencer, K.D.,Thoden, J.B.,Holden, H.M. (登録日: 2021-09-08, 公開日: 2021-09-22, 最終更新日: 2023-10-18)

主引用文献

Griffiths, W.A.,Spencer, K.D.,Thoden, J.B.,Holden, H.M.
Biochemical investigation of an N-acetyltransferase from Helicobacter pullorum.
Protein Sci., 30:2418-2432, 2021

PubMed Abstract: N-acetylated sugars are often found, for example, on the lipopolysaccharides of Gram-negative bacteria, on the S-layers of Gram-positive bacteria, and on the capsular polysaccharides. Key enzymes involved in their biosynthesis are the sugar N-acetyltransferases. Here, we describe a structural and functional analysis of one such enzyme from Helicobacter pullorum, an emerging pathogen that may be associated with gastroenteritis and gallbladder and liver diseases. For this analysis, the gene BA919-RS02330 putatively encoding an N-acetyltransferase was cloned, and the corresponding protein was expressed and purified. A kinetic analysis demonstrated that the enzyme utilizes dTDP-3-amino-3,6-dideoxy-d-glucose as a substrate as well as dTDP-3-amino-3,6-dideoxy-d-galactose, albeit at a reduced rate. In addition to this kinetic analysis, a similar enzyme from Helicobacter bilis was cloned and expressed, and its kinetic parameters were determined. Seven X-ray crystallographic structures of various complexes of the H. pullorum wild-type enzyme (or the C80T variant) were determined to resolutions of 1.7 Å or higher. The overall molecular architecture of the H. pullorum N-acetyltransferase places it into the Class II left-handed-β-helix superfamily (LβH). Taken together, the data presented herein suggest that 3-acetamido-3,6-dideoxy-d-glucose (or the galactose derivative) is found on either the H. pullorum O-antigen or in another of its complex glycoconjugates. A BLAST search suggests that more than 50 non-pylori Helicobacter spp. have genes encoding N-acetyltransferases. Given that there is little information concerning the complex glycans in non-pylori Helicobacter spp. and considering their zoonotic potential, our results provide new biochemical insight into these pathogens.

PubMed: 34651380
DOI: 10.1002/pro.4207

実験手法

X-RAY DIFFRACTION (1.4 Å)