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Crystal structure ofescherichia coliqor quinone oxidoreductase complexed with nadph

Journal Article


Abstract


  • The crystal structure of the homodimer of quinone oxidoreductase fromEscherichia colihas been determined using the multiple isomorphous replacement method at 2.2 AÅ 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.f2 f2 Abbreviations used: QOR, quinone oxidoreductase; LADH, liver alcohol dehydrogenase; GDH, glucose dehydrogenase; MIR, multiple isomorphous replacement; SA, simulated annealing; NCS, non-crystallographic symmetry. © 1995 Academic Press Limited.

Publication Date


  • 1995

Citation


  • Thorn, J. M., Barton, J. D., Dixon, N. E., Ollis, D. L., & Edwards, K. J. (1995). Crystal structure ofescherichia coliqor quinone oxidoreductase complexed with nadph. Journal of Molecular Biology, 249(4), 785-799. doi:10.1006/jmbi.1995.0337

Scopus Eid


  • 2-s2.0-0028977970

Start Page


  • 785

End Page


  • 799

Volume


  • 249

Issue


  • 4

Abstract


  • The crystal structure of the homodimer of quinone oxidoreductase fromEscherichia colihas been determined using the multiple isomorphous replacement method at 2.2 AÅ 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.f2 f2 Abbreviations used: QOR, quinone oxidoreductase; LADH, liver alcohol dehydrogenase; GDH, glucose dehydrogenase; MIR, multiple isomorphous replacement; SA, simulated annealing; NCS, non-crystallographic symmetry. © 1995 Academic Press Limited.

Publication Date


  • 1995

Citation


  • Thorn, J. M., Barton, J. D., Dixon, N. E., Ollis, D. L., & Edwards, K. J. (1995). Crystal structure ofescherichia coliqor quinone oxidoreductase complexed with nadph. Journal of Molecular Biology, 249(4), 785-799. doi:10.1006/jmbi.1995.0337

Scopus Eid


  • 2-s2.0-0028977970

Start Page


  • 785

End Page


  • 799

Volume


  • 249

Issue


  • 4