2AMJ

Crystal Structure of Modulator of Drug Activity B from Escherichia coli O157:H7

2AMJ の概要

• エントリーDOI: 10.2210/pdb2amj/pdb
• 関連するPDBエントリー: 2B3D
• 分子名称: Modulator of drug activity B (2 entities in total)
• 機能のキーワード: oxidoreductase, menadione, dt-diaphorase, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93801.46

構造登録者

Adams, M.A.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2005-08-09, 公開日: 2006-07-18, 最終更新日: 2024-11-13)

主引用文献

Adams, M.A.,Jia, Z.
Modulator of drug activity B from Escherichia coli: crystal structure of a prokaryotic homologue of DT-diaphorase.
J.Mol.Biol., 359:455-465, 2006

PubMed Abstract: Modulator of drug activity B (MdaB) is a putative member of the DT-diaphorase family of NAD(P)H:oxidoreductases that afford cellular protection against quinonoid compounds. While there have been extensive investigations of mammalian homologues, putative prokaryotic members of this enzyme family have received little attention. The three-dimensional crystal structure of apo-MdaB reported herein exhibits significant structural similarity to a number of flavoproteins, including the mammalian DT-diaphorases. We have shown by mass spectrometry that the endogenously associated cofactor is flavin adenine dinucleotide and we present here the structure of MdaB in complex with this compound. Growth of Escherichia coli carrying null mutations in the genes encoding MdaB or quinol monooxygenase, the gene for which shares the mdaB promoter, were not affected by the presence of menadione. However, over-expression of recombinant quinol monooxygenase conferred a state of resistance against both tetracycline and adriamycin. This work suggests that the redox cycle formed by these proteins protects E. coli from the toxic effects of polyketide compounds rather than the oxidative stress of menadione alone.

PubMed: 16630630
DOI: 10.1016/j.jmb.2006.03.053

実験手法

X-RAY DIFFRACTION (1.8 Å)