Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP)
Journal Article
·
· Acta Crystallogr. F
- UAB
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 {angstrom} resolution. Multiwavelength anomalous diffraction (MAD) data were collected utilizing the Zn{sup 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.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- UNIVERSITY
- OSTI ID:
- 1034548
- Journal Information:
- Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (11) ; 11, 2011 Vol. 67; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- ENGLISH
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