Work

Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe 4 S 4 ] Protein IspH

Year: 2013

Type: article

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.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201208469

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

Institutions: Center for Integrated Protein Science Munich, Technical University of Munich, University of Illinois Urbana-Champaign, Saarland University

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: Structure, Function and Inhibition of [4Fe-4S] Proteins, G580921589

OpenAlex ID: W2107432183

FWCI: 2.405

Cites: 26

Cited by: 29

Related to: 10