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2Y0F

STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27

2Y0F の概要
エントリーDOI10.2210/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: 21167158
DOI: 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)
構造検証レポート
Validation report summary of 2y0f
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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