7M7A
Legionella pneumophila MavQ lipid kinase
Summary for 7M7A
| Entry DOI | 10.2210/pdb7m7a/pdb |
| Descriptor | Phosphoinositide 3-kinase MavQ, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | transferase |
| Biological source | Legionella pneumophila subsp. pneumophila |
| Total number of polymer chains | 4 |
| Total formula weight | 275723.34 |
| Authors | Tomchick, D.R.,Tagliabracci, V.S.,Hsieh, T.S.,Lopez, V.A. (deposition date: 2021-03-27, release date: 2021-04-28, Last modification date: 2024-05-22) |
| Primary citation | Hsieh, T.S.,Lopez, V.A.,Black, M.H.,Osinski, A.,Pawlowski, K.,Tomchick, D.R.,Liou, J.,Tagliabracci, V.S. Dynamic remodeling of host membranes by self-organizing bacterial effectors. Science, 372:935-941, 2021 Cited by PubMed Abstract: During infection, intracellular bacterial pathogens translocate a variety of effectors into host cells that modify host membrane trafficking for their benefit. We found a self-organizing system consisting of a bacterial phosphoinositide kinase and its opposing phosphatase that formed spatiotemporal patterns, including traveling waves, to remodel host cellular membranes. The effector MavQ, a phosphatidylinositol (PI) 3-kinase, was targeted to the endoplasmic reticulum (ER). MavQ and the PI 3-phosphatase SidP, even in the absence of other bacterial components, drove rapid PI 3-phosphate turnover on the ER and spontaneously formed traveling waves that spread along ER subdomains inducing vesicle and tubule budding. Thus, bacteria can exploit a self-organizing membrane-targeting mechanism to hijack host cellular structures for survival. PubMed: 33927055DOI: 10.1126/science.aay8118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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