5KVQ

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

Summary for 5KVQ

• Entry DOI: 10.2210/pdb5kvq/pdb
• Related: 5KVS
• Descriptor: Irp3 protein, 1,2-ETHANEDIOL, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: imine reductase, oxidoreductase, thiazolinyl, siderophore, yersiniabactin
• Biological source: Yersinia enterocolitica
• Total number of polymer chains: 2
• Total formula weight: 87464.65

Authors

Meneely, K.M.,Lamb, A.L. (deposition date: 2016-07-15, release date: 2016-09-21, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)