2Y0F
STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27
Summary for 2Y0F
| Entry DOI | 10.2210/pdb2y0f/pdb |
| Descriptor | 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE, IRON/SULFUR CLUSTER (3 entities in total) |
| Functional Keywords | oxidoreductase, isoprenoid biosynthesis, non-mevalonate pathway |
| Biological source | THERMUS THERMOPHILUS |
| Total number of polymer chains | 4 |
| Total formula weight | 178530.94 |
| Authors | Rekittke, I.,Nonaka, T.,Wiesner, J.,Demmer, U.,Warkentin, E.,Jomaa, H.,Ermler, U. (deposition date: 2010-12-02, release date: 2011-01-26, Last modification date: 2024-05-08) |
| Primary citation | Rekittke, I.,Nonaka, T.,Wiesner, J.,Demmer, U.,Warkentin, E.,Jomaa, H.,Ermler, U. Structure of the E-1-Hydroxy-2-Methyl-But-2-Enyl-4-Diphosphate Synthase (Gcpe) from Thermus Thermophilus. FEBS Lett., 585:447-, 2011 Cited by PubMed 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. PubMed: 21167158DOI: 10.1016/J.FEBSLET.2010.12.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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