3RIE

The structure of Plasmodium falciparum spermidine synthase in complex with 5'-methylthioadenosine and N-(3-aminopropyl)-trans-cyclohexane-1,4-diamine

Summary for 3RIE

• Entry DOI: 10.2210/pdb3rie/pdb
• Descriptor: Spermidine synthase, 5'-DEOXY-5'-METHYLTHIOADENOSINE, trans-N-(3-aminopropyl)cyclohexane-1,4-diamine, ... (6 entities in total)
• Functional Keywords: rossmann-like fold, rossmann fold, spermidine synthesis, aminopropyl transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 3
• Total formula weight: 98597.89

Authors

Williams, M.,Sprenger, J.,Persson, L.,Louw, A.I.,Birkholtz, L.,Al-Karadaghi, S. (deposition date: 2011-04-13, release date: 2012-04-25, Last modification date: 2023-09-13)

Primary citation

Burger, P.B.,Williams, M.,Sprenger, J.,Reeksting, S.B.,Botha, M.,Muller, I.B.,Joubert, F.,Birkholtz, L.M.,Louw, A.I.
A novel inhibitor of Plasmodium falciparum spermidine synthase: a twist in the tail.
Malar J, 14:54-54, 2015

PubMed Abstract: Plasmodium falciparum is the most pathogenic of the human malaria parasite species and a major cause of death in Africa. It's resistance to most of the current drugs accentuates the pressing need for new chemotherapies. Polyamine metabolism of the parasite is distinct from the human pathway making it an attractive target for chemotherapeutic development. Plasmodium falciparum spermidine synthase (PfSpdS) catalyzes the synthesis of spermidine and spermine. It is a major polyamine flux-determining enzyme and spermidine is a prerequisite for the post-translational activation of P. falciparum eukaryotic translation initiation factor 5A (elF5A). The most potent inhibitors of eukaryotic SpdS's are not specific for PfSpdS.

PubMed: 25651815
DOI: 10.1186/s12936-015-0572-z

Experimental method

X-RAY DIFFRACTION (1.9 Å)