ArticleStructure (London, England : 1993)2013
IcmQ in the Type 4b secretion system contains an NAD+ binding domain.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- A survey of ADP-ribosyltransferase families in the pathogenic Legionella.BMC genomics · 2025Article
- Evolutionary Dissection of the Dot/Icm System Based on Comparative Genomics of 58 Legionella Species.Genome biology and evolution · 2019Article
- Crystal structure of the Legionella pneumophila Lem10 effector reveals a new member of the HD protein superfamily.Proteins · 2015Article
- Biological Diversity and Evolution of Type IV Secretion Systems.Current topics in microbiology and immunologyArticle
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9 authors at 3 institutions in 1 country.
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Abstract
A Type 4b secretion system (T4bSS) is required for Legionella growth in alveolar macrophages. IcmQ associates with IcmR, binds to membranes, and has a critical role in the T4bSS. We have now solved a crystal structure of IcmR-IcmQ to further our understanding of this complex. This structure revealed an amphipathic four-helix bundle, formed by IcmR and the N-terminal domain of IcmQ, which is linked to a novel C-terminal domain of IcmQ (Qc) by a linker helix. The Qc domain has structural homology with ADP ribosyltransferase domains in certain bacterial toxins and binds NAD(+) with a dissociation constant in the physiological range. Structural homology and molecular dynamics were used to identify an extended NAD(+) binding site on Qc, and the resulting model was tested by mutagenesis and binding assays. Based on the data, we suggest that IcmR-IcmQ binds to membranes, where it may interact with, or perhaps modify, a protein in the T4bSS when NAD(+) is bound.
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