2011年2月
Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus
FEBS LETTERS
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- 巻
- 585
- 号
- 3
- 開始ページ
- 447
- 終了ページ
- 451
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.febslet.2010.12.012
- 出版者・発行元
- ELSEVIER SCIENCE BV
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 (alpha beta)(8) barrel. The great [4Fe-4S] cluster-substrate distance implicates large-scale domain rearrangements during the reaction cycle.
Structured summary:
gcpE binds to gcpE by x-ray crystallography (View interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Structured summary:
gcpE binds to gcpE by x-ray crystallography (View interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.febslet.2010.12.012
- ISSN : 0014-5793
- Web of Science ID : WOS:000286657700001