7XQL
complex structure of LegA15 with GNP
Summary for 7XQL
| Entry DOI | 10.2210/pdb7xql/pdb |
| Descriptor | Ankyrin repeat-containing protein, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (3 entities in total) |
| Functional Keywords | legionella penumophila effector, gtpase, toxin |
| Biological source | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 104427.56 |
| Authors | Chen, T.T.,Lin, Y.L. (deposition date: 2022-05-07, release date: 2023-05-17, Last modification date: 2023-12-20) |
| Primary citation | Chen, T.T.,Lin, Y.,Zhang, S.,Liu, S.,Song, L.,Zhong, W.,Luo, Z.Q.,Han, A. Atypical Legionella GTPase effector hijacks host vesicular transport factor p115 to regulate host lipid droplet. Sci Adv, 8:eadd7945-eadd7945, 2022 Cited by PubMed Abstract: The intracellular bacterial pathogen uses hundreds of effector proteins to manipulate multiple processes of the host cells to establish a replicative niche known as -containing vacuole (LCV). Biogenesis of the LCV has been known to depend on host small guanosine triphosphatases (GTPases), but whether bacterial effector GTPases are also involved remains unknown. Here, we show that an ankyrin repeat containing effector LegA15 localizes directly in host lipid droplets (LDs), leading to Golgi apparatus fragmentation of the host cells by hijacking the host vesicular transport factor p115. LegA15 is a GTPase with a unique catalytic mechanism, unlike any eukaryotic small GTPases. Moreover, the effector LegA15 co-opts p115 to modulate homeostasis of the host LDs in its GTPase-dependent manner. Together, our data reveal that an atypical GTPase effector regulates the host LDs through impeding the vesicle secretion system of the host cells for intracellular life cycle of . PubMed: 36525490DOI: 10.1126/sciadv.add7945 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.272 Å) |
Structure validation
Download full validation report
