8H2C

Crystal structure of the pseudaminic acid synthase PseI from Campylobacter jejuni

8H2C の概要

• エントリーDOI: 10.2210/pdb8h2c/pdb
• 分子名称: Pseudaminic acid synthase, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: pseudaminic acid synthase, tim barrel fold, type iii antifreeze-like domain, condensation reaction, biosynthetic protein
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157174.97

構造登録者

Song, W.S.,Park, M.A.,Ki, D.U.,Yoon, S.I. (登録日: 2022-10-05, 公開日: 2022-11-09, 最終更新日: 2024-04-03)

主引用文献

Song, W.S.,Park, M.A.,Ki, D.U.,Yoon, S.I.
Structural analysis of the pseudaminic acid synthase PseI from Campylobacter jejuni.
Biochem.Biophys.Res.Commun., 635:252-258, 2022

PubMed Abstract: Campylobacter jejuni PseI is a pseudaminic acid synthase that condenses the 2,4-diacetamido-2,4,6-trideoxy-l-altrose sugar (6-deoxy AltdiNAc) and phosphoenolpyruvate to generate pseudaminic acid, a sialic acid-like 9-carbon backbone α-keto sugar. Pseudaminic acid is conjugated to cell surface proteins and lipids and plays a key role in the mobility and virulence of C. jejuni and other pathogenic bacteria. To provide insights into the catalytic mechanism of PseI, we performed a structural study on PseI. PseI forms a two-domain structure and assembles into a domain-swapped homodimer. The PseI dimer has two cavities, each of which accommodates a metal ion using conserved histidine residues. A comparative analysis of structures and sequences suggests that the cavity of PseI functions as an active site that binds the 6-deoxy AltdiNAc and phosphoenolpyruvate substrates and mediates their condensation. Furthermore, we propose the substrate binding-induced structural rearrangement of PseI and predict 6-deoxy AltdiNAc recognition residues that are specific to PseI.

PubMed: 36283338
DOI: 10.1016/j.bbrc.2022.10.050

実験手法

X-RAY DIFFRACTION (2.9 Å)