3QWB

Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1 complexed with NADPH

Summary for 3QWB

• Entry DOI: 10.2210/pdb3qwb/pdb
• Related: 3QWA
• Descriptor: Probable quinone oxidoreductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: rossmann fold, quinone oxidoreductases, nadph, cytoplasm and nucleus, oxidoreductase
• Biological source: Saccharomyces cerevisiae (yeast)
• Total number of polymer chains: 4
• Total formula weight: 151696.42

Authors

Guo, P.C.,Ma, X.X.,Bao, Z.Z.,Chen, Y.X.,Zhou, C.Z. (deposition date: 2011-02-28, release date: 2012-02-08, Last modification date: 2023-11-01)

Primary citation

Guo, P.C.,Ma, X.X.,Bao, Z.Z.,Ma, J.D.,Chen, Y.,Zhou, C.Z.
Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1
J.Struct.Biol., 176:112-118, 2011

PubMed Abstract: Quinone oxidoreductase (QOR EC1.6.5.5) catalyzes the reduction of quinone to hydroxyquinone using NADPH as a cofactor. Here we present the crystal structure of the ζ-crystallin-like QOR Zta1 from Saccharomycescerevisiae in apo-form at 2.00 Å and complexed with NADPH at 1.59 Å resolution. Zta1 forms a homodimer, with each subunit containing a catalytic and a cofactor-binding domain. Upon NADPH binding to the interdomain cleft, the two domains shift towards each other, producing a better fit for NADPH, and tightening substrate binding. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis defined a potential quinone-binding site that determines the stringent substrate specificity. Moreover, multiple-sequence alignment and kinetics assays implied that a single-residue change from Arg in lower organisms to Gly in vertebrates possibly resulted in elevation of enzymatic activity of ζ-crystallin-like QORs throughout evolution.

PubMed: 21820057
DOI: 10.1016/j.jsb.2011.07.010

Experimental method

X-RAY DIFFRACTION (1.59 Å)