3JYN

Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH

Summary for 3JYN

• Entry DOI: 10.2210/pdb3jyn/pdb
• Related: 3JYL
• Descriptor: Quinone oxidoreductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: rossmann fold, protein-nadph complex, oxidoreductase
• Biological source: Pseudomonas syringae pv. tomato
• Total number of polymer chains: 1
• Total formula weight: 35123.50

Authors

Pan, X.,Zhang, H.,Gao, Y.,Li, M.,Chang, W. (deposition date: 2009-09-22, release date: 2010-01-12, Last modification date: 2023-11-01)

Primary citation

Pan, X.,Zhang, H.,Gao, Y.,Li, M.,Chang, W.
Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH
Biochem.Biophys.Res.Commun., 390:597-602, 2009

PubMed Abstract: Zeta-crystallin-like quinone oxidoreductase is NAD(P)H-dependent and catalyzes one-electron reduction of certain quinones to generate semiquinone. Here we present the crystal structures of zeta-crystallin-like quinone oxidoreductase from Pseudomonas syringae pv. tomato DC3000 (PtoQOR) and its complexes with NADPH determined at 2.4 and 2.01A resolutions, respectively. PtoQOR forms as a homologous dimer, each monomer containing two domains. In the structure of the PtoQOR-NADPH complex, NADPH locates in the groove between the two domains. NADPH binding causes obvious conformational changes in the structure of PtoQOR. The putative substrate-binding site of PtoQOR is wider than that of Escherichia coli and Thermus thermophilus HB8. Activity assays show that PtoQOR has weak 1,4-benzoquinone catalytic activity, and very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. We propose a model to explain the conformational changes which take place during reduction reactions catalyzed by PtoQOR.

PubMed: 19818736
DOI: 10.1016/j.bbrc.2009.10.012

Experimental method

X-RAY DIFFRACTION (2.01 Å)