1D5C

CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM RAB6 COMPLEXED WITH GDP

1D5C の概要

• エントリーDOI: 10.2210/pdb1d5c/pdb
• 分子名称: RAB6 GTPASE, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: g-protein, gtpase, rab, rab6, vesicular trafficking, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19205.32

構造登録者

Chattopadhyay, D.,Langsley, G.,Carson, M.,Recacha, R.,DeLucas, L.,Smith, C. (登録日: 1999-10-06, 公開日: 2000-08-30, 最終更新日: 2024-10-16)

主引用文献

Chattopadhyay, D.,Langsley, G.,Carson, M.,Recacha, R.,DeLucas, L.,Smith, C.
Structure of the nucleotide-binding domain of Plasmodium falciparum rab6 in the GDP-bound form.
Acta Crystallogr.,Sect.D, 56:937-944, 2000

PubMed Abstract: Rab proteins are small Ras-like GTPases which play important roles in regulating intracellular vesicle trafficking. The nucleotide-binding domain of Rab6 from the malaria parasite Plasmodium falciparum was crystallized with GDP bound to the active site. The MAD phasing technique was used to determine the crystal structure to 2.3 A resolution. Comparisons of the structure of GDP-bound PfRab6 with the recently determined structures of Rab3A in complex with either a GTP analog or with GTP and Rabphillin present structural evidence supporting the traditional model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues homologous to those distinguishing human Rab6 isoforms, which differ in binding to Rabkinesin-6 in human cells, are located next to the recognized complementarity-determining region (CDR) and constitute a conceptual broadening of that domain. Despite significant observable differences in Golgi ultrastructure, the Rab6 core structure and switch mechanism appear highly conserved when compared with murine Rab3a structures. A significant difference between the PfRab6 and higher eukaryotic Rabs may be the lack of CDR features that allow binding interactions with Rabkinesin-type effectors.

PubMed: 10944329
DOI: 10.1107/S0907444900007575

実験手法

X-RAY DIFFRACTION (2.3 Å)