Open AccessStructure of the catalytic domain of Plasmodium falciparum ARF GTPase‐activating protein (ARFGAP)
Author(s) -
Cook William J.,
Senkovich Olga,
Chattopadhyay Debasish
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111032507
Subject(s) - plasmodium falciparum , dimer , gtpase , crystal structure , domain (mathematical analysis) , zinc finger , gtpase activating protein , resolution (logic) , chemistry , crystallography , biology , biochemistry , malaria , gene , g protein , signal transduction , mathematical analysis , mathematics , organic chemistry , artificial intelligence , transcription factor , computer science , immunology
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.