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| Item Type: | Article |
|---|---|
| Title: | The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion |
| Creators Name: | Schulte, K., Pawlowski, N., Faelber, K., Fröhlich, C., Howard, J. and Daumke, O. |
| Abstract: | BACKGROUND: 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. RESULTS: We 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. CONCLUSIONS: The 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. |
| Keywords: | Innate Immunity, IRG Proteins, GTPase, Dynamin Superfamily, Dimerization, Oligomerization, Animals, Mice |
| Source: | BMC Biology |
| ISSN: | 1741-7007 |
| Publisher: | BioMed Central |
| Volume: | 14 |
| Number: | 1 |
| Page Range: | 14 |
| Date: | 2 March 2016 |
| Official Publication: | https://doi.org/10.1186/s12915-016-0236-7 |
| PubMed: | View item in PubMed |
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