Solution Conformations and Dynamics of Substrate-Bound Cytochrome P450 MycG.

ABSTRACT: MycG is a P450 monooxygenase that catalyzes the sequential hydroxylation and epoxidation of mycinamicin IV (M-IV), the last two steps in the biosynthesis of mycinamicin II, a macrolide antibiotic isolated from Micromonospora griseorubida. The crystal structure of MycG with M-IV bound was previously determined but showed the bound substrate in an orientation that did not rationalize the observed regiochemistry of M-IV hydroxylation. Nuclear magnetic resonance paramagnetic relaxation enhancements provided evidence of an orientation of M-IV in the MycG active site more compatible with the observed chemistry, but substrate-induced changes in the enzyme structure were not characterized. We now describe the use of amide ¹H-¹⁵N residual dipolar couplings as experimental rest

SUBMITTER: Tietz DR 

PROVIDER: S-EPMC5520640 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature