3B6M

WrbA from Escherichia coli, second crystal form

Summary for 3B6M

• Entry DOI: 10.2210/pdb3b6m/pdb
• Related: 3B6I 3B6J 3B6K
• Descriptor: Flavoprotein wrbA, FLAVIN MONONUCLEOTIDE, TRIS-HYDROXYMETHYL-METHYL-AMMONIUM, ... (5 entities in total)
• Functional Keywords: flavoproteins, nadh:quinone oxidoreductase, fmn, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 44411.75

Authors

Andrade, S.L.A.,Patridge, E.V.,Ferry, J.G.,Einsle, O. (deposition date: 2007-10-29, release date: 2007-12-11, Last modification date: 2023-08-30)

Primary citation

Andrade, S.L.,Patridge, E.V.,Ferry, J.G.,Einsle, O.
Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli.
J.Bacteriol., 189:9101-9107, 2007

PubMed Abstract: The flavoprotein WrbA, originally described as a tryptophan (W) repressor-binding protein in Escherichia coli, has recently been shown to exhibit the enzymatic activity of a NADH:quinone oxidoreductase. This finding points toward a possible role in stress response and in the maintenance of a supply of reduced quinone. We have determined the three-dimensional structure of the WrbA holoprotein from E. coli at high resolution (1.66 A), and we observed a characteristic, tetrameric quaternary structure highly similar to the one found in the WrbA homologs of Deinococcus radiodurans and Pseudomonas aeruginosa. A similar tetramer was originally observed in an iron-sulfur flavoprotein involved in the reduction of reactive oxygen species. Together with other, recently characterized proteins such as YhdA or YLR011wp (Lot6p), these tetrameric flavoproteins may constitute a large family with diverse functions in redox catalysis. WrbA binds substrates at an active site that provides an ideal stacking environment for aromatic moieties, while providing a pocket that is structured to stabilize the ADP part of an NADH molecule in its immediate vicinity. Structures of WrbA in complex with benzoquinone and NADH suggest a sequential binding mechanism for both molecules in the catalytic cycle.

PubMed: 17951395
DOI: 10.1128/JB.01336-07

Experimental method

X-RAY DIFFRACTION (1.85 Å)