1.14.14.33 | to 2.15 A resolution. The structure shows a domain-like insertion into a TIM-barrel, which might serve as a flexible lid for the active site. Docking of MgEDTA2- into EmoA identifies an intricate hydrogen bond network connected to Tyr71, which should lower its pKa. Tyr71, along with nearby Glu70 and a peroxy flavin, facilitates a keto-enol transition of the leaving acetyl group of EDTA. The interaction between EmoA and oxidoreductase EmoB enhances both EmoA and EmoB activities probably through coupled channelling of FMNH2 |
739091 |