Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus

Rekittke, Ingo; Jomaa, Hassan H.; Ermler, Ulrich

doi:10.1016/j.febslet.2012.07.070

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Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus

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Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Rekittke, I., Jomaa, H. H., & Ermler, U. (2012). Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus. FEBS Letters, 586(19), 3452-3457. doi:10.1016/j.febslet.2012.07.070.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D54E-B

Abstract

Isoprenoid precursor biosynthesis occurs through the mevalonate or the methylerythritol phosphate (MEP) pathway, used i.e., by humans and by many human pathogens, respectively. In the MEP pathway, 2-C-methyl-D-erythritol-2,4-cyclo-diphosphate (MEcPP) is converted to (E)-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate (HMBPP) by the iron–sulfur cluster enzyme HMBPP synthase (GcpE). The presented X-ray structure of the GcpE–MEcPP complex from Thermus thermophilus at 1.55 Å resolution provides valuable information about the catalytic mechanism and for rational inhibitor design. MEcPP binding inside the TIM-barrel funnel induces a 60° rotation of the [4Fe–4S] cluster containing domain onto the TIM-barrel entrance. The apical iron of the [4Fe–4S] cluster ligates with the C3 oxygen atom of MEcPP.