2b3d

Crystal structure of Modulator of Drug activity B in complex with flavin adenine dinucleotide

spinqualitylabelsall models 2b3d, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b3d is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD Related: 2amj Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Modulator of drug activity B from Escherichia coli: crystal structure of a prokaryotic homologue of DT-diaphorase.,Adams MA, Jia Z J Mol Biol. 2006 Jun 2;359(2):455-65. Epub 2006 Apr 7. PMID:16630630 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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