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Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1

Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1,10.1016/j.jsb.2011.07.010,Journal of Structu

Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1  
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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 2.00Å and complexed with NADPH at 1.59Å 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.
Journal: Journal of Structural Biology - J STRUCT BIOL , vol. 176, no. 1, pp. 112-118, 2011
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