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

Chair of Biochemistry

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

22 Scopus citations

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

Keywords

IspH
LytB
bioinorganic chemistry
metalloenzymes
terpenoids

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1002/anie.201208469

Cite this

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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.",

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AU - Eisenreich, Wolfgang

AU - Bacher, Adelbert

AU - Oldfield, Eric

AU - Groll, Michael

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KW - metalloenzymes

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