Crystal structure of Legionella DotD: insights into the relationship between type IVB and type II/III secretion systems.

Clicks: 308
ID: 100109
2010
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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.
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nakano2010crystalplos Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Nakano, Noboru;Kubori, Tomoko;Kinoshita, Miki;Imada, Katsumi;Nagai, Hiroki;
Journal PLoS pathogens
Year 2010
DOI
10.1371/journal.ppat.1001129
URL
http://europepmc.org/articles/PMC2951367?pdf=render
Keywords
membrane proteins assembly pathway effector translocation nanomachine

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