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  Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus

Rekittke, I., Nonaka, T., Wiesner, J., Demmer, U., Warkentin, E., Jomaa, H., et al. (2011). Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus. FEBS Letters, 585(3), 447-451. doi:10.1016/j.febslet.2010.12.012.

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 Creators:
Rekittke, Ingo1, Author
Nonaka, Tsuyoshi2, Author              
Wiesner, Jochen1, Author
Demmer, Ulrike2, Author              
Warkentin, Eberhard2, Author              
Jomaa, Hassan1, Author
Ermler, Ulrich2, Author              
Affiliations:
1Institut für Klinische Immunologie und Transfusionsmedizin, Justus-Liebig-Universität Giessen, Langhansstraße 7, 35392 Giessen, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Non-mevalonate pathway; E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase; Iron–sulfur cluster; X-ray structure; Drug design
 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

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Language(s): eng - English
 Dates: 2010-12-062010-11-092010-12-082010-12-152011-02-04
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.febslet.2010.12.012
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 585 (3) Sequence Number: - Start / End Page: 447 - 451 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501