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

Academic Article

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. © 2011 International Union of Crystallography. All rights reserved.
  • Digital Object Identifier (doi)

    Author List

  • Cook WJ; Senkovich O; Chattopadhyay D
  • Start Page

  • 1339
  • End Page

  • 1344
  • Volume

  • 67
  • Issue

  • 11