Dynamin superfamily members are large GTPases conserved through evolution mainly described as mechanochemical enzymes involved in membrane scission events. The Plasmodium falciparum dynamin-2 (Pfdyn2) gene was cloned from the FcB1 strain. PfDYN2 belongs to the dynamin-like protein subgroup of the dynamin superfamily since it possesses a large GTPase domain together with the conserved dynamin_M and GED domains. Recombinant PfDYN2 was able to bind GTP, to hydrolyze GTP into GDP and to self-associate in low-salt conditions. PfDYN2 expression was restricted to schizonts where it localized in punctuate structures within the parasite cytoplasm. PfDYN2 partly co-localized with markers of the parasite endoplasmic reticulum, Golgi apparatus and apicoplast, suggesting it could be implicated in vesicular trafficking and/or organelle fission events known to occur during the last hours of the parasite development in erythrocytes. PfDYN2 and the previously described PfDYN1 are the only two dynamin superfamily members identified in the P. falciparum genome and the available data suggest that this situation is conserved in the Apicomplexa phylum.