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.

Ämnesord

NATURVETENSKAP  -- Biologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

Nyckelord

vitamin K

menaquinone

peripheral membrane proteins

soluble quinones

membrane quinones

chemotherapeutics

shikimate

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)