Ontology highlight
ABSTRACT:
SUBMITTER: Ryan KS
PROVIDER: S-EPMC3983088 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Ryan Katherine S KS Chakraborty Sumita S Howard-Jones Annaleise R AR Walsh Christopher T CT Ballou David P DP Drennan Catherine L CL
Biochemistry 20081201 51
RebC is a putative flavin hydroxylase functioning together with RebP to carry out a key step in the biosynthesis of rebeccamycin. To probe the mechanism of flavin-based chemistry in RebC, we solved the structure of RebC with reduced flavin. Upon flavin reduction, the RebC crystal undergoes a change in its unit cell dimension concurrent with a 5 A movement of the isoalloxazine ring, positioning the flavin ring adjacent to the substrate-binding pocket. Additionally, a disordered helix becomes orde ...[more]