Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus |
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| Authors: | Rekittke Ingo Nonaka Tsuyoshi Wiesner Jochen Demmer Ulrike Warkentin Eberhard Jomaa Hassan Ermler Ulrich |
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| Affiliation: | aInstitut für Klinische Immunologie und Transfusionsmedizin, Justus-Liebig-Universität Giessen, Langhansstraße 7, 35392 Giessen, Germany;bMax-Planck-Institut für Biophysik, Max-von-Laue-Straße 3, D-60438 Frankfurt am Main, Germany |
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| Abstract: | Isoprenoids are biosynthesized via the mevalonate or the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathways the latter being used by most pathogenic bacteria, some parasitic protozoa, plant plastids, but not by animals. We determined the X-ray structure of the homodimeric [4Fe–4S] cluster carrying E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) of Thermus thermophilus which catalyzes the penultimate reaction of the MEP pathway and is therefore an attractive target for drug development. The [4Fe–4S] cluster ligated to three cysteines and one glutamate is encapsulated at the intersubunit interface. The substrate binding site lies in front of an (αβ)8 barrel. The great [4Fe–4S] cluster-substrate distance implicates large-scale domain rearrangements during the reaction cycle.Structured summarygcpEbinds to gcpE by x-ray crystallography (View interaction) |
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| Keywords: | Abbreviations: GcpE, E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase MEP, 2-C-methyl- font-variant: small-caps" >d-erythritol-4-phosphate MEcPP, 2-C-methyl- font-variant: small-caps" >d-erythritol-2,4-cyclo-diphosphate HMBPP, E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate |
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