3lrp | pdb_00003lrp
Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1
Structural highlights
FunctionARF1_PLAF7 Small GTPase involved in protein trafficking between different compartments (PubMed:21045287). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Regulates the transport of N-acylated AK2 to the parasitophorous vacuole membrane (PubMed:33604307). May be involved in the activation of lipid kinase PIP5K (PubMed:19171150).[UniProtKB:P84077][1] [2] [3] Publication Abstract from PubMedVesicular trafficking may play a crucial role in the pathogenesis and survival of the malaria parasite. ADP-ribosylation factors (ARFs) are among the major components of vesicular trafficking pathways in eukaryotes. The crystal structure of ARF1 GTPase from Plasmodium falciparum has been determined in the GDP-bound conformation at 2.5 A resolution and is compared with the structures of mammalian ARF1s. Structure of Plasmodium falciparum ADP-ribosylation factor 1.,Cook WJ, Smith CD, Senkovich O, Holder AA, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1426-31. Epub 2010 Oct 27. PMID:21045287[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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