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Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Thorn JM,Barton JD,Dixon NE,Ollis DL,Edwards KJ

doi

10.1006/jmbi.1995.0337

subject

Has Abstract

pub_date

1995-06-16 00:00:00

pages

785-99

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(85)70337-3

journal_volume

249

pub_type

杂志文章

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