1OKT

X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum

Summary for 1OKT

• Entry DOI: 10.2210/pdb1okt/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, FORMIC ACID (3 entities in total)
• Functional Keywords: gst, plasmodium falciparum, transferase
• Biological source: PLASMODIUM FALCIPARUM
• Total number of polymer chains: 2
• Total formula weight: 49864.20

Authors

Fritz-Wolf, K.,Becker, A.,Rahlfs, s.,Harwaldt, P.,Schirmer, R.H.,Kabsch, W.,Becker, K. (deposition date: 2003-07-29, release date: 2003-11-20, Last modification date: 2024-05-08)

Primary citation

Fritz-Wolf, K.,Becker, A.,Rahlfs, S.,Harwaldt, P.,Schirmer, R.H.,Kabsch, W.,Becker, K.
X-Ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium Falciparum
Proc.Natl.Acad.Sci.USA, 100:13821-, 2003

PubMed Abstract: GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is highly abundant in the parasite, its activity was found to be increased in chloroquine-resistant cells, and it has been shown to act as a ligandin for parasitotoxic hemin. Thus, the enzyme represents a promising target for antimalarial drug development. We now have solved the crystal structure of PfGST at a resolution of 1.9 A. The homodimeric protein of 26 kDa per subunit represents a GST form that cannot be assigned to any of the known GST classes. In comparison to other GSTs, and, in particular, to the human isoforms, PfGST possesses a shorter C-terminal section resulting in a more solvent-accessible binding site for the hydrophobic and amphiphilic substrates. The structure furthermore reveals features in this region that could be exploited for the design of specific PfGST inhibitors.

PubMed: 14623980
DOI: 10.1073/PNAS.2333763100

Experimental method

X-RAY DIFFRACTION (1.9 Å)