2b3d
From Proteopedia
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|PDB= 2b3d |SIZE=350|CAPTION= <scene name='initialview01'>2b3d</scene>, resolution 2.1Å | |PDB= 2b3d |SIZE=350|CAPTION= <scene name='initialview01'>2b3d</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2amj|2AMJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3d OCA], [http://www.ebi.ac.uk/pdbsum/2b3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b3d RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Adams, M A.]] | [[Category: Adams, M A.]] | ||
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
| - | [[Category: | + | [[Category: dt-diaphorase]] |
| + | [[Category: menadione reductase]] | ||
[[Category: modulator of drug activity b]] | [[Category: modulator of drug activity b]] | ||
| - | [[Category: nad(p)h:oxidoreductase | + | [[Category: nad(p)h:oxidoreductase]] |
| + | [[Category: quinone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:51 2008'' |
Revision as of 23:00, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Related: | 2AMJ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Modulator of Drug activity B in complex with flavin adenine dinucleotide
Overview
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.
About this Structure
2B3D is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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