ArticleProtein science : a publication of the Protein Society2018
X-ray crystal structures of the type IVb secretion system DotB ATPases.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Comparative Analysis of T4SS Molecular Architectures.Journal of microbiology and biotechnology · 2023Review
- Structure and Function of the Dot/Icm T4SS.bioRxiv : the preprint server for biology · 2023Article
- Molecular architecture of bacterial type IV secretion systems.PLoS pathogens · 2022Review
- Recent advances in structural studies of the Legionella pneumophila Dot/Icm type IV secretion system.Microbiology and immunology · 2022Review
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- The TraK accessory factor activates substrate transfer through the pKM101 type IV secretion system independently of its role in relaxosome assembly.Molecular microbiology · 2020Article
- Article
- Multiple conformations facilitate PilT function in the type IV pilus.Nature communications · 2019Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective.EMBO reports · 2019Review
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2 authors at 2 institutions in 1 country.
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Abstract
Human infections by the intracellular bacterial pathogen Legionella pneumophila result in a severe form of pneumonia, the Legionnaire's disease. L. pneumophila utilizes a Type IVb secretion (T4bS) system termed "dot/icm" to secrete protein effectors to the host cytoplasm. The dot/icm system is powered at least in part by a functionally critical AAA+ ATPase, a protein called DotB, thought to belong to the VirB11 family of proteins. Here we present the crystal structure of DotB at 3.19 Å resolution, in its hexameric form. We observe that DotB is in fact a structural intermediate between VirB11 and PilT family proteins, with a PAS-like N-terminal domain coupled to a RecA-like C-terminal domain. It also shares critical structural elements only found in PilT. The structure also reveals two conformers, termed α and β, with an αβαβαβ configuration. The existence of α and β conformers in this class of proteins was confirmed by solving the structure of DotB from another bacterial pathogen, Yersinia, where, intriguingly, we observed an ααβααβ configuration. The two conformers co-exist regardless of the nucleotide-bound states of the proteins. Our investigation therefore reveals that these ATPases can adopt a wider range of conformational states than was known before, shedding new light on the extraordinary spectrum of conformations these ATPases can access to carry out their function. Overall, the structure of DotB provides a template for further rational drug design to develop more specific antibiotics to tackle Legionnaire's disease. PDB Code(s): Will; be; provided.
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