Structures of fluoro, amino, and thiol inhibitors bound to the [Fe 4S4] protein IspH

Ingrid Span; Ke Wang; Weixue Wang; Johann Jauch; Wolfgang Eisenreich; Adelbert Bacher; Eric Oldfield; Michael Groll

doi:10.1002/anie.201208469

Structures of fluoro, amino, and thiol inhibitors bound to the [Fe ₄S₄] protein IspH

Ingrid Span, Ke Wang, Weixue Wang, Johann Jauch, Wolfgang Eisenreich, Adelbert Bacher, Eric Oldfield, Michael Groll

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	2118-2121
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	7
DOIs	https://doi.org/10.1002/anie.201208469
State	Published - Feb 11 2013

Keywords

IspH
LytB
bioinorganic chemistry
metalloenzymes
terpenoids

ASJC Scopus subject areas

Catalysis
General Chemistry

Online availability

10.1002/anie.201208469

Library availability

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Cite this

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AU - Eisenreich, Wolfgang

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AU - Oldfield, Eric

AU - Groll, Michael

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