3SUB

Crystal structure of the catalytic domain of Plasmodium falciparum ARF GTPase activating protein

Summary for 3SUB

• Entry DOI: 10.2210/pdb3sub/pdb
• Descriptor: ADP-ribosylation factor GTPase-activating protein, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: gtpase-activating protein, protein trafficking, hydrolase activator
• Biological source: Plasmodium falciparum 3D7
• Total number of polymer chains: 2
• Total formula weight: 37558.74

Authors

Cook, W.J.,Chattopadhyay, D. (deposition date: 2011-07-11, release date: 2011-11-09, Last modification date: 2024-02-28)

Primary citation

Cook, W.J.,Senkovich, O.,Chattopadhyay, D.
Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).
Acta Crystallogr.,Sect.F, 67:1339-1344, 2011

PubMed 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.

PubMed: 22102228
DOI: 10.1107/S1744309111032507

Experimental method

X-RAY DIFFRACTION (2.4 Å)