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Structural Studies of The N‐terminal Domain of Plasmodium Falciparum Copper P‐ATPase (PfCuP‐ATPase)
Author(s) -
Kisaka Javan,
Huffman David
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.lb180
Subject(s) - atpase , plasmodium falciparum , p type atpase , circular dichroism , biochemistry , biology , biophysics , atp7a , chemistry , computational biology , microbiology and biotechnology , malaria , enzyme , immunology
Plasmodium falciparum is one of the four parasites that cause malaria in humans. Resistance of malarial parasites to some of existing drugs calls for a need to develop new therapeutic agents. Integral membrane proteins which are metal transporters are potential targets for drug development. PfCuP‐ATPase, a copper‐transporting ATPase in Plasmodium parasites, is a potential target for new antimalarials. PfCuP‐ATPase has one copper binding motif in the N‐terminal region. The C‐terminal portion of the protein has ten predicted trans‐membrane helices and multiple inserts of unknown function. The structural organization of PfCuP‐ATPase has not been elucidated. Our objective is to understand the structure and function of the N‐terminal region. We have applied protein modeling tools to predict structured sub‐domains in the N‐terminal domain of PfCuP‐ATPase (Fig. 1 &2). Circular Dichroism and Nuclear Magnetic Resonance spectroscopy methods were used to study the biophysical properties of the predicted domains (Fig. 3). Our preliminary results indicate that the N‐terminal domain structured regions may have multiple ferredoxin folds. We have been able to determine that there exists three independent subdomains in the N‐terminal portion of PfCuP‐ATPase.