PMID:7602590

Citation	Thorn, JM, Barton, JD, Dixon, NE, Ollis, DL and Edwards, KJ (1995) Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J. Mol. Biol. 249:785-99
Abstract	The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 A resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase.
Links	PubMed Online version:10.1006/jmbi.1995.0337
Keywords	Amino Acid Sequence; Base Sequence; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli/metabolism; Models, Molecular; Molecular Sequence Data; NADH, NADPH Oxidoreductases/chemistry; NADH, NADPH Oxidoreductases/metabolism; NADP/metabolism; Protein Structure, Secondary
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