Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents



  history
ID: 680386.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum
Authors:Rekittke, Ingo; Olkhova, Elena; Wiesner, Jochen; Demmer, Ulrike; Warkentin, Eberhard; Jomaa, Hassan; Ermler, Ulrich
Language:English
Date of Publication (YYYY-MM-DD):2013-12-11
Title of Journal:FEBS Letters
Journal Abbrev.:FEBS Lett.
Volume:587
Issue / Number:24
Start Page:3968
End Page:3972
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Terpenoid precursor biosynthesis occurs in human and many pathogenic organisms via the mevalonate and 2-C-methyl-D-erythritol-4-phosphate (MEP) pathways, respectively. We determined the X-ray structure of the Fe/S containing (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase (LytB) of the pathogenic protozoa Plasmodium falciparum which catalyzes the terminal step of the MEP pathway. The cloverleaf fold and the active site of P. falciparum LytB corresponds to those of the Aquifex aeolicus and Escherichia coli enzymes. Its distinct electron donor [2Fe–2S] ferredoxin was modeled to its binding site by docking calculations. The presented structural data provide a platform for a rational search of anti-malarian drugs.
Free Keywords:Isoprenoid biosynthesis; LytB; X-ray structure; Drug design; Plasmodium falciparum
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
External Affiliations:Medizinische Klinik IV (Hämatologie), Justus-Liebig-Universität Giessen, Klinikstrasse 33, D-35392 Giessen, Germany
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.