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3ADY

Crystal structure of DotD from Legionella

Summary for 3ADY
Entry DOI10.2210/pdb3ady/pdb
DescriptorDotD (2 entities in total)
Functional Keywords3-layer(bab) sandwich, mth1598-like, proton transport
Biological sourceLegionella pneumophila
Total number of polymer chains1
Total formula weight16191.57
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 citationNakano, 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: 20949065
DOI: 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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