3LRP

Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1

Summary for 3LRP

• Entry DOI: 10.2210/pdb3lrp/pdb
• Related: 3LRO
• Descriptor: ADP-ribosylation factor 1, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: adp-ribosylation factor, protein trafficking, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, myristate, nucleotide-binding, protein transport, transport, signaling protein
• Biological source: Plasmodium falciparum
• Cellular location: Golgi apparatus (By similarity): Q94650
• Total number of polymer chains: 1
• Total formula weight: 21502.40

Authors

Cook, W.J.,Chattopadhyay, D. (deposition date: 2010-02-11, release date: 2010-11-10, Last modification date: 2023-09-06)

Primary citation

Cook, W.J.,Smith, C.D.,Senkovich, O.,Holder, A.A.,Chattopadhyay, D.
Structure of Plasmodium falciparum ADP-ribosylation factor 1.
Acta Crystallogr.,Sect.F, 66:1426-1431, 2010

PubMed Abstract: Vesicular 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 Å resolution and is compared with the structures of mammalian ARF1s.

PubMed: 21045287
DOI: 10.1107/S1744309110036997

Experimental method

X-RAY DIFFRACTION (2.5 Å)