3ADY
Crystal structure of DotD from Legionella
Summary for 3ADY
| Entry DOI | 10.2210/pdb3ady/pdb |
| Descriptor | DotD (2 entities in total) |
| Functional Keywords | 3-layer(bab) sandwich, mth1598-like, proton transport |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 16191.57 |
| Authors | Imada, K.,Nakano, N.,Kubori, T.,Kinoshita, M.,Nagai, H. (deposition date: 2010-01-29, release date: 2010-11-03, Last modification date: 2024-03-13) |
| Primary citation | Nakano, N.,Kubori, T.,Kinoshita, M.,Imada, K.,Nagai, H. Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems Plos Pathog., 6:e1001129-e1001129, 2010 Cited by PubMed Abstract: 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. PubMed: 20949065DOI: 10.1371/journal.ppat.1001129 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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