6JYG

Crystal Structure of L-threonine dehydrogenase from Phytophthora infestans

Summary for 6JYG

• Entry DOI: 10.2210/pdb6jyg/pdb
• Descriptor: L-threonine 3-dehydrogenase, putative, CITRATE ANION, 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL, ... (5 entities in total)
• Functional Keywords: l-threonine dehydrogenase, oxidoreductase
• Biological source: Phytophthora infestans (strain T30-4) (Potato late blight fungus)
• Total number of polymer chains: 6
• Total formula weight: 235871.86

Authors

Yoneda, K.,Sakuraba, H.,Ohshima, T. (deposition date: 2019-04-26, release date: 2020-04-01, Last modification date: 2023-11-22)

Primary citation

Yoneda, K.,Nagano, R.,Mikami, T.,Sakuraba, H.,Fukui, K.,Araki, T.,Ohshima, T.
Catalytic properties and crystal structure of UDP-galactose 4-epimerase-like l-threonine 3-dehydrogenase from Phytophthora infestans.
Enzyme.Microb.Technol., 140:109627-109627, 2020

PubMed Abstract: We report, for the first time, the three-dimensional structure and biochemical properties of a UDP-galactose 4-epimerase-like l-threonine 3-dehydrogenase (GalE-like L-ThrDH) from Phytophthora infestans, a plant disease-causing fungus. We identified GalE-like L-ThrDH using Kyoto Encyclopedia of Genes and Genomes (KEGG) database as a candidate target for the development of a new fungicide. The GalE-like L-ThrDH gene was expressed in Escherichia coli, and its product was purified and characterized. N-Acetylglycine was found to act as a competitive inhibitor of the enzyme (Ki =0.18 mM). The crystal structure of the unique hexameric GalE-like L-ThrDH was determined using the molecular replacement method at a resolution of 2.3 Å, in the presence of NAD and citrate, an analogue of the substrate. Based on the molecular docking simulation, N-acetylglycine molecule was modeled into the active site and the binding mode and inhibition mechanism of N-acetylglycine were elucidated.

PubMed: 32912687
DOI: 10.1016/j.enzmictec.2020.109627

Experimental method

X-RAY DIFFRACTION (2.31 Å)