Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems.
The Dot/Icm type IVB secretion system (T4BSS) is a pivotal determinant of Legionella pneumophila pathogenesis. L. pneumophila translocate more than 100 effector proteins into host cytoplasm using Dot/Icm T4BSS, modulating host cellular functions to establish a replicative niche within host cells. Th...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2010-10-01
|
| Series: | PLoS Pathogens |
| Online Access: | http://europepmc.org/articles/PMC2951367?pdf=render |
| _version_ | 1818359343186182144 |
|---|---|
| author | Noboru Nakano Tomoko Kubori Miki Kinoshita Katsumi Imada Hiroki Nagai |
| author_facet | Noboru Nakano Tomoko Kubori Miki Kinoshita Katsumi Imada Hiroki Nagai |
| author_sort | Noboru Nakano |
| collection | DOAJ |
| description | The Dot/Icm type IVB secretion system (T4BSS) is a pivotal determinant of Legionella pneumophila pathogenesis. L. pneumophila translocate more than 100 effector proteins into host cytoplasm using Dot/Icm T4BSS, modulating host cellular functions to establish a replicative niche within host cells. The T4BSS core complex spanning the inner and outer membranes is thought to be made up of at least five proteins: DotC, DotD, DotF, DotG and DotH. DotH is the outer membrane protein; its targeting depends on lipoproteins DotC and DotD. However, the core complex structure and assembly mechanism are still unknown. Here, we report the crystal structure of DotD at 2.0 Å resolution. The structure of DotD is distinct from that of VirB7, the outer membrane lipoprotein of the type IVA secretion system. In contrast, the C-terminal domain of DotD is remarkably similar to the N-terminal subdomain of secretins, the integral outer membrane proteins that form substrate conduits for the type II and the type III secretion systems (T2SS and T3SS). A short β-segment in the otherwise disordered N-terminal region, located on the hydrophobic cleft of the C-terminal domain, is essential for outer membrane targeting of DotH and Dot/Icm T4BSS core complex formation. These findings uncover an intriguing link between T4BSS and T2SS/T3SS. |
| first_indexed | 2024-12-13T20:43:23Z |
| format | Article |
| id | doaj.art-42c79aa9e5aa43ed9bd1fc8fcd851a23 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-13T20:43:23Z |
| publishDate | 2010-10-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-42c79aa9e5aa43ed9bd1fc8fcd851a232022-12-21T23:32:05ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742010-10-01610e100112910.1371/journal.ppat.1001129Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems.Noboru NakanoTomoko KuboriMiki KinoshitaKatsumi ImadaHiroki NagaiThe Dot/Icm type IVB secretion system (T4BSS) is a pivotal determinant of Legionella pneumophila pathogenesis. L. pneumophila translocate more than 100 effector proteins into host cytoplasm using Dot/Icm T4BSS, modulating host cellular functions to establish a replicative niche within host cells. The T4BSS core complex spanning the inner and outer membranes is thought to be made up of at least five proteins: DotC, DotD, DotF, DotG and DotH. DotH is the outer membrane protein; its targeting depends on lipoproteins DotC and DotD. However, the core complex structure and assembly mechanism are still unknown. Here, we report the crystal structure of DotD at 2.0 Å resolution. The structure of DotD is distinct from that of VirB7, the outer membrane lipoprotein of the type IVA secretion system. In contrast, the C-terminal domain of DotD is remarkably similar to the N-terminal subdomain of secretins, the integral outer membrane proteins that form substrate conduits for the type II and the type III secretion systems (T2SS and T3SS). A short β-segment in the otherwise disordered N-terminal region, located on the hydrophobic cleft of the C-terminal domain, is essential for outer membrane targeting of DotH and Dot/Icm T4BSS core complex formation. These findings uncover an intriguing link between T4BSS and T2SS/T3SS.http://europepmc.org/articles/PMC2951367?pdf=render |
| spellingShingle | Noboru Nakano Tomoko Kubori Miki Kinoshita Katsumi Imada Hiroki Nagai Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. PLoS Pathogens |
| title | Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. |
| title_full | Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. |
| title_fullStr | Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. |
| title_full_unstemmed | Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. |
| title_short | Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems. |
| title_sort | crystal structure of legionella dotd insights into the relationship between type ivb and type ii iii secretion systems |
| url | http://europepmc.org/articles/PMC2951367?pdf=render |
| work_keys_str_mv | AT noborunakano crystalstructureoflegionelladotdinsightsintotherelationshipbetweentypeivbandtypeiiiiisecretionsystems AT tomokokubori crystalstructureoflegionelladotdinsightsintotherelationshipbetweentypeivbandtypeiiiiisecretionsystems AT mikikinoshita crystalstructureoflegionelladotdinsightsintotherelationshipbetweentypeivbandtypeiiiiisecretionsystems AT katsumiimada crystalstructureoflegionelladotdinsightsintotherelationshipbetweentypeivbandtypeiiiiisecretionsystems AT hirokinagai crystalstructureoflegionelladotdinsightsintotherelationshipbetweentypeivbandtypeiiiiisecretionsystems |