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Publication Abstract from PubMed
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.
Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.,Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ J Mol Biol. 1995 Jun 16;249(4):785-99. PMID:7602590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J Mol Biol. 1995 Jun 16;249(4):785-99. PMID:7602590 doi:http://dx.doi.org/10.1006/jmbi.1995.0337
