1QOR

CRYSTAL STRUCTURE OF ESCHERICHIA COLI QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH

1QOR の概要

• エントリーDOI: 10.2210/pdb1qor/pdb
• 分子名称: QUINONE OXIDOREDUCTASE, SULFATE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72109.13

構造登録者

Thorn, J.M.,Barton, J.D.,Dixon, N.E.,Ollis, D.L.,Edwards, K.J. (登録日: 1995-02-14, 公開日: 1995-06-03, 最終更新日: 2024-02-14)

主引用文献

Thorn, J.M.,Barton, J.D.,Dixon, N.E.,Ollis, D.L.,Edwards, K.J.
Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.
J.Mol.Biol., 249:785-799, 1995

PubMed 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.

PubMed: 7602590
DOI: 10.1006/jmbi.1995.0337

実験手法

X-RAY DIFFRACTION (2.2 Å)