5FPH

The GTPase domains of the immunity-related Irga6 dimerize in a parallel head-to-head fashion

Summary for 5FPH

Entry DOI	10.2210/pdb5fph/pdb
Descriptor	INTERFERON-INDUCIBLE GTPASE 1, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	hydrolase, irga6, gmppnp, innate immunity, irg proteins, gtpase, dynamin superfamily, oligomerization
Biological source	MUS MUSCULUS (HOUSE MOUSE)
Cellular location	Cytoplasm: Q9QZ85
Total number of polymer chains	7
Total formula weight	346497.76
Authors	Schulte, K.,Pawlowski, N.,Faelber, K.,Froehlich, C.,Howard, J.,Daumke, O. (deposition date: 2015-11-30, release date: 2016-02-10, Last modification date: 2024-11-06)
Primary citation	Schulte, K.,Pawlowski, N.,Faelber, K.,Froehlich, C.,Howard, J.,Daumke, O. The Immunity-Related Gtpase Irga6 Dimerizes in a Parallel Head-to-Head Fashion. Bmc Biol., 14:14-, 2016 Cited by PubMed Abstract: The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens. Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation. Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization. PubMed: 26934976 DOI: 10.1186/S12915-016-0236-7 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.2 Å)

Structure validation