title: Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).
abstract: The crystal structure of the catalytic domain of the ADP ribosylation factor GTPase-activating protein (ARFGAP) from Plasmodium falciparum has been determined and refined to 2.4 Å resolution. Multiwavength anomalous diffraction (MAD) data were collected utilizing the Zn(2+) ion bound at the zinc-finger domain and were used to solve the structure. The overall structure of the domain is similar to those of mammalian ARFGAPs. However, several amino-acid residues in the area where GAP interacts with ARF1 differ in P. falciparum ARFGAP. Moreover, a number of residues that form the dimer interface in the crystal structure are unique in P. falciparum ARFGAP.
authors.affiliation: Department of Medicine, University of Alabama at Birmingham, CBSE-250, 1015 18th Street South, Birmingham, AL 35294, USA.
authors.forename: William J
authors.initials: WJ
authors.lastname: Cook
authors.forename: Olga
authors.initials: O
authors.lastname: Senkovich
authors.forename: Debasish
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D020727:ADP-Ribosylation Factors / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000201:enzymology*; D016415:Sequence Alignment
chemical_list: D020727:ADP-Ribosylation Factors
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