5UIN

X-ray structure of the W305A variant of the FdtF N-formyltransferase from salmonella enteric O60

5UIN の概要

• エントリーDOI: 10.2210/pdb5uin/pdb
• 関連するPDBエントリー: 5uij 5uik 5uil 5uim
• 分子名称: Formyltransferase, THYMIDINE-5'-DIPHOSPHATE, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: ankyrin repeat, lipopolysaccharide, o-antigen, transferase
• 由来する生物種: Salmonella choleraesuis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94524.81

構造登録者

Woodford, C.R.,Thoden, J.B.,Holden, H.M. (登録日: 2017-01-14, 公開日: 2017-03-22, 最終更新日: 2023-10-04)

主引用文献

Woodford, C.R.,Thoden, J.B.,Holden, H.M.
Molecular architecture of an N-formyltransferase from Salmonella enterica O60.
J. Struct. Biol., 200:267-278, 2017

PubMed Abstract: N-formylated sugars are found on the lipopolysaccharides of various pathogenic Gram negative bacteria including Campylobacter jejuni 81116, Francisella tularensis, Providencia alcalifaciens O30, and Providencia alcalifaciens O40. The last step in the biosynthetic pathways for these unusual sugars is catalyzed by N-formyltransferases that utilize N-formyltetrahydrofolate as the carbon source. The substrates are dTDP-linked amino sugars with the functional groups installed at either the C-3' or C-4' positions of the pyranosyl rings. Here we describe a structural and enzymological investigation of the putative N-formyltransferase, FdtF, from Salmonella enterica O60. In keeping with its proposed role in the organism, the kinetic data reveal that the enzyme is more active with dTDP-3-amino-3,6-dideoxy-d-galactose than with dTDP-3-amino-3,6-dideoxy-d-glucose. The structural data demonstrate that the enzyme contains, in addition to the canonical N-formyltransferase fold, an ankyrin repeat moiety that houses a second dTDP-sugar binding pocket. This is only the second time an ankyrin repeat has been shown to be involved in small molecule binding. The research described herein represents the first structural analysis of a sugar N-formyltransferase that specifically functions on dTDP-3-amino-3,6-dideoxy-d-galactose in vivo and thus adds to our understanding of these intriguing enzymes.

PubMed: 28263875
DOI: 10.1016/j.jsb.2017.03.002

実験手法

X-RAY DIFFRACTION (2.2 Å)