4B65

A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP(H)

4B65 の概要

• エントリーDOI: 10.2210/pdb4b65/pdb
• 関連するPDBエントリー: 4B63 4B64 4B66 4B67 4B68 4B69
• 分子名称: L-ORNITHINE N5 MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, siderophore, flavin
• 由来する生物種: ASPERGILLUS FUMIGATUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58955.09

構造登録者

Franceschini, S.,Fedkenheuer, M.,Vogelaar, N.J.,Robinson, H.H.,Sobrado, P.,Mattevi, A. (登録日: 2012-08-09, 公開日: 2012-10-03, 最終更新日: 2023-12-20)

主引用文献

Franceschini, S.,Fedkenheuer, M.,Vogelaar, N.J.,Robinson, H.H.,Sobrado, P.,Mattevi, A.
Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases.
Biochemistry, 51:7043-, 2012

PubMed Abstract: SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes.

PubMed: 22928747
DOI: 10.1021/BI301072W

実験手法

X-RAY DIFFRACTION (2.32 Å)