WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.
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.
Carey
Jannette
J
Chemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA. jcarey@princeton.edu
Brynda
Jiri
J
Wolfová
Julie
J
Grandori
Rita
R
Gustavsson
Tobias
T
Ettrich
Rüdiger
R
Smatanová
Ivana Kutá
IK
D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005418:Flavodoxin / Q000737:chemistry*; D008958:Models, Molecular; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry*; D017510:Protein Folding; D012097:Repressor Proteins / Q000737:chemistry*
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D005418:Flavodoxin; D012097:Repressor Proteins; C081759:WrbA protein, E coli; D016660:NAD(P)H Dehydrogenase (Quinone)