9FTB

Aeromonas caviae CMP-Pse5A7Ac Synthetase

9FTB の概要

• エントリーDOI: 10.2210/pdb9ftb/pdb
• 分子名称: NeuA (2 entities in total)
• 機能のキーワード: carbohydrate synthesis, pseudaminic acid synthesis, cmp-transferase, transferase
• 由来する生物種: Aeromonas caviae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28011.84

構造登録者

Keenan, T.,Fascione, M.A.,Cowan, A.R.,Hemsworth, G.R. (登録日: 2024-06-24, 公開日: 2024-10-09, 最終更新日: 2024-12-18)

主引用文献

Keenan, T.,Cowan, A.R.,Flack, E.K.P.,Hatton, N.E.,Walklett, A.J.,Thomas, G.H.,Hemsworth, G.R.,Fascione, M.A.
Structural dissection of the CMP-pseudaminic acid synthetase, PseF.
Structure, 32:2399-, 2024

PubMed Abstract: Pseudaminic acid is a non-mammalian sugar found in the surface glycoconjugates of many bacteria, including several human pathogens, and is a virulence factor thought to facilitate immune evasion. The final step in the biosynthesis of the nucleotide activated form of the sugar, CMP-Pse5Ac7Ac is performed by a CMP-Pse5Ac7Ac synthetase (PseF). Here we present the biochemical and structural characterization of PseF from Aeromonas caviae (AcPseF), with AcPseF displaying metal-dependent activity over a broad pH and temperature range. Upon binding to CMP-Pse5Ac7Ac, AcPseF undergoes dynamic movements akin to other CMP-ulosonic acid synthetases. The enzyme clearly discriminates Pse5Ac7Ac from other ulosonic acids, through active site interactions with side-chain functional groups and by positioning the molecule in a hydrophobic pocket. Finally, we show that AcPseF binds the CMP-Pse5Ac7Ac side chain in the lowest energy conformation, a trend that we observed in the structures of other enzymes of this class.

PubMed: 39393361
DOI: 10.1016/j.str.2024.09.017

実験手法

X-RAY DIFFRACTION (1.9 Å)