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Crystal structure of the catalytic domain of Plasmodium falciparum ARF GTPase activating proteinCrystal structure of the catalytic domain of Plasmodium falciparum ARF GTPase activating protein
Structural highlights
Publication Abstract from PubMedThe 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 A 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. Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).,Cook WJ, Senkovich O, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1339-44., Epub 2011 Oct 25. PMID:22102228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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