ArticleBMC biology2016
The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion.
Article in BMC biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Structural insights into GM4951 as a lipid droplet GTPase regulating hepatic lipid metabolism.Nature communications · 2025Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Toxoplasma rhoptry proteins that affect encephalitis outcome.Cell death discovery · 2023Review
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- ATPase activity of DFCP1 controls selective autophagy.Nature communications · 2023Article
- Structural basis of IRGB10 oligomerization by GTP hydrolysis.Frontiers in immunology · 2023Article
- Loss of immunity-related GTPase GM4951 leads to nonalcoholic fatty liver disease without obesity.Nature communications · 2022Article
- Structural basis of membrane recognition ofLife science alliance · 2022Article
- Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption.Communications biology · 2021Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Evolution of Cell-Autonomous Effector Mechanisms in Macrophages versus Non-Immune Cells.Microbiology spectrum · 2016Review
- Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.Biopolymers · 2016Review
- Facilitation of Endosomal Recycling by an IRG Protein Homolog Maintains Apical Tubule Structure in Caenorhabditis elegans.Genetics · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe 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.
resultsWe determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog. Contrary to the previous model, the structure shows that the GTPase domains dimerize in a parallel fashion. The nucleotides in the center of the interface participate in dimerization by forming symmetric contacts with each other and with the switch I region of the opposing Irga6 molecule. The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site. Further dimerization contacts involve switch II, the G4 helix and the trans stabilizing loop.
conclusionsThe Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members. This study contributes important insights into the assembly and catalytic mechanisms of IRG proteins as prerequisite to understand their anti-microbial action.
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