4N7B

Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate reductase from Plasmodium falciparum

Summary for 4N7B

• Entry DOI: 10.2210/pdb4n7b/pdb
• Descriptor: LytB, FE3-S4 CLUSTER, SULFATE ION, ... (6 entities in total)
• Functional Keywords: iron-sulfur-cluster binding, oxidoreductase
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 1
• Total formula weight: 64062.25

Authors

Rekittke, I.,Jomaa, H.,Ermler, U. (deposition date: 2013-10-15, release date: 2013-11-20, Last modification date: 2024-02-28)

Primary citation

Rekittke, I.,Olkhova, E.,Wiesner, J.,Demmer, U.,Warkentin, E.,Jomaa, H.,Ermler, U.
Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum.
Febs Lett., 587:3968-3972, 2013

PubMed Abstract: 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.

PubMed: 24188825
DOI: 10.1016/j.febslet.2013.10.029

Experimental method

X-RAY DIFFRACTION (2.198 Å)