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Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe 4 S 4 ] Protein IspH
Author(s) -
Span Ingrid,
Wang Ke,
Wang Weixue,
Jauch Johann,
Eisenreich Wolfgang,
Bacher Adelbert,
Oldfield Eric,
Groll Michael
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201208469
Subject(s) - chemistry , thiol , computer science , computational biology , service (business) , key (lock) , sulfur , biochemistry , world wide web , information retrieval , nanotechnology , biology , materials science , organic chemistry , economy , computer security , economics
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.