5KVQ

NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica

5KVQ の概要

• エントリーDOI: 10.2210/pdb5kvq/pdb
• 関連するPDBエントリー: 5KVS
• 分子名称: Irp3 protein, 1,2-ETHANEDIOL, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: imine reductase, oxidoreductase, thiazolinyl, siderophore, yersiniabactin
• 由来する生物種: Yersinia enterocolitica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87464.65

構造登録者

Meneely, K.M.,Lamb, A.L. (登録日: 2016-07-15, 公開日: 2016-09-21, 最終更新日: 2023-10-04)

主引用文献

Meneely, K.M.,Ronnebaum, T.A.,Riley, A.P.,Prisinzano, T.E.,Lamb, A.L.
Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.
Biochemistry, 55:5423-5433, 2016

PubMed Abstract: Thiazolinyl imine reductases catalyze the NADPH-dependent reduction of a thiazoline to a thiazolidine, a required step in the formation of the siderophores yersiniabactin (Yersinia spp.) and pyochelin (Pseudomonas aeruginosa). These stand-alone nonribosomal peptide tailoring domains are structural homologues of sugar oxidoreductases. Two closed structures of the thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) are presented here: an NADP(+)-bound structure to 1.45 Å resolution and a holo structure to 1.28 Å resolution with NADP(+) and a substrate analogue bound. Michaelis-Menten kinetics were measured using the same substrate analogue and the homologue from P. aeruginosa, PchG. The data presented here support the hypothesis that tyrosine 128 is the likely general acid residue for catalysis and also highlight the phosphopantetheine tunnel for tethering of the substrate to the nonribosomal peptide synthetase module during assembly line biosynthesis of the siderophore.

PubMed: 27601130
DOI: 10.1021/acs.biochem.6b00735

実験手法

X-RAY DIFFRACTION (1.45 Å)