Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe4S4] Protein IspH

Angewandte Chemie, 2013, DOI: 10.1002/anie.201208469, Volume 52, Issue 7, pages 2118–2121 published on 11.02.2013

Angewandte Chemie, online article

The iron–sulfur protein IspH catalyzes a key step in isoprenoid biosynthesis in bacteria and malaria parasites. Crystal structures of IspH complexed with three substrate analogues reveal their mode of binding and suggest new routes to inhibitor design.  

TU München
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry