2Y0F
STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27
2Y0F の概要
エントリーDOI | 10.2210/pdb2y0f/pdb |
分子名称 | 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE, IRON/SULFUR CLUSTER (3 entities in total) |
機能のキーワード | oxidoreductase, isoprenoid biosynthesis, non-mevalonate pathway |
由来する生物種 | THERMUS THERMOPHILUS |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 178530.94 |
構造登録者 | Rekittke, I.,Nonaka, T.,Wiesner, J.,Demmer, U.,Warkentin, E.,Jomaa, H.,Ermler, U. (登録日: 2010-12-02, 公開日: 2011-01-26, 最終更新日: 2024-05-08) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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