6exe | pdb_00006exe

Crystal structure of DotM cytoplasmic domain (residues 153-380),R217E

spinqualitylabelsall models 6exe, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6exe is a 2 chain structure with sequence from Legph. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, MES Gene: icmP, lpg0445 (LEGPH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Legionella 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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