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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.

SUBMITTER: Cook WJ

PROVIDER: S-EPMC3212447 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).

Cook William J WJ Senkovich Olga O Chattopadhyay Debasish D

Acta crystallographica. Section F, Structural biology and crystallization communications 20111025 Pt 11

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 ...[more]

PMID: 22102228

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