6C4M

Yersinopine dehydrogenase (YpODH) - NADP+ bound

6C4M の概要

• エントリーDOI: 10.2210/pdb6c4m/pdb
• 分子名称: Yersinopine dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: opine dehydrogenase metallophore siderophore, yersinopine pseudopaline staphylopine, oxidoreductase
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53858.46

構造登録者

McFarlane, J.S.,Davis, C.L.,Lamb, A.L. (登録日: 2018-01-12, 公開日: 2018-04-11, 最終更新日: 2024-03-13)

主引用文献

McFarlane, J.S.,Davis, C.L.,Lamb, A.L.
Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenase.
J. Biol. Chem., 293:8009-8019, 2018

PubMed Abstract: Opine dehydrogenases (ODHs) from the bacterial pathogens , , and perform the final enzymatic step in the biosynthesis of a new class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Growing evidence indicates an important role for this pathway in metal acquisition and virulence, including in lung and burn-wound infections () and in blood and heart infections (). Here, we present kinetic and structural characterizations of these three opine dehydrogenases. A steady-state kinetic analysis revealed that the three enzymes differ in α-keto acid and NAD(P)H substrate specificity and nicotianamine-like substrate stereoselectivity. The structural basis for these differences was determined from five ODH X-ray crystal structures, ranging in resolution from 1.9 to 2.5 Å, with or without NADP bound. Variation in hydrogen bonding with NADPH suggested an explanation for the differential recognition of this substrate by these three enzymes. Our analysis further revealed candidate residues in the active sites required for binding of the α-keto acid and nicotianamine-like substrates and for catalysis. This work reports the first structural kinetic analyses of enzymes involved in opine metallophore biosynthesis in three important bacterial pathogens of humans.

PubMed: 29618515
DOI: 10.1074/jbc.RA118.002007

実験手法

X-RAY DIFFRACTION (1.94 Å)