Publications by authors named "Julie Wolfova"
Structural organization of WrbA in apo- and holoprotein crystals.
Biochim Biophys Acta
September 2009
Article Synopsis
- - The study refines and analyzes various crystal forms of the E. coli protein WrbA, revealing structural differences between its holoprotein (with FMN bound) and apoprotein (without FMN).
- - Comparisons with flavodoxin structures show that WrbA, despite differences in structure and residue types, exhibits similar local changes upon FMN binding, highlighting conserved features across these proteins.
- - The findings suggest that WrbA should be viewed as a key member of the flavodoxin family, rather than an atypical branch, due to shared structural characteristics and functional similarities.
The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.
View Article and Find Full Text PDFCrystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide.
Acta Crystallogr Sect F Struct Biol Cryst Commun
July 2007
The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity.
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