6exa
Crystal structure of DotM cytoplasmic domain (residues 153-380), double mutant R196E/R197ECrystal structure of DotM cytoplasmic domain (residues 153-380), double mutant R196E/R197E
Structural highlights
Publication Abstract from PubMedLegionella pneumophila, a causative agent of pneumonia, utilizes the Type 4B secretion (T4BS) system to translocate over 300 effectors into the host cell during infection. T4BS systems are encoded by a large gene cluster termed dot/icm, three components of which, DotL, DotM, and DotN, form the "coupling complex", which serves as a platform for recruitment of effector proteins. One class of effectors includes proteins containing Glu-rich/E-block sequences at their C terminus. However, the protein or region of the coupling complex mediating recruitment of such effectors is unknown. Here we present the crystal structure of DotM. This all alpha-helical structure exhibits patches of positively charged residues. We show that these regions form binding sites for acidic Glu-rich peptides and that mutants targeting these patches are defective in vivo in the translocation of acidic Glu-rich motif-containing effectors. We conclude that DotM forms the interacting surface for recruitment of acidic Glu-rich motif-containing Legionella effectors. Legionella DotM structure reveals a role in effector recruiting to the Type 4B secretion system.,Meir A, Chetrit D, Liu L, Roy CR, Waksman G Nat Commun. 2018 Feb 6;9(1):507. doi: 10.1038/s41467-017-02578-x. PMID:29410427[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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