Open AccessPurification, crystallization and preliminary X‐ray analysis of the aspartate aminotransferase of Plasmodium falciparum
Author(s) -
Jain Rishabh,
Jordanova Rositsa,
Müller Ingrid B.,
Wrenger Carsten,
Groves Matthew R.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110003933
Subject(s) - plasmodium falciparum , crystallization , x ray , chemistry , biology , malaria , immunology , physics , organic chemistry , quantum mechanics
Aspartate aminotransferases (EC 2.6.1.1) catalyse the conversion of aspartate and α‐ketoglutarate to oxaloacetate and glutamate in a reversible manner. Thus, the aspartate aminotransferase of Plasmodium falciparum ( Pf AspAT) plays a central role in the transamination of amino acids. Recent findings suggest that Pf AspAT may also play a pivotal role in energy metabolism and the de novo biosynthesis of pyrimidines. While therapeutics based upon the inhibition of other proteins in these pathways are already used in the treatment of malaria, the advent of multidrug‐resistant strains has limited their efficacy. The presence of Pf AspAT in these pathways may offer additional opportunities for the development of novel therapeutics. In order to gain a deeper understanding of the function and role of Pf AspAT, it has been expressed and purified to homogeneity. The successful crystallization of Pf AspAT, the collection of a 2.8 Å diffraction data set and initial attempts to solve the structure using molecular replacement are reported.