6EXD
Crystal structure of DotM cytoplasmic domain (residues 153-380) SeMet derivative
Summary for 6EXD
Entry DOI | 10.2210/pdb6exd/pdb |
Descriptor | IcmP (DotM) (2 entities in total) |
Functional Keywords | membrane protein, secretion system, type 4 secretion system, legionella pneumophila, protein binding |
Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
Total number of polymer chains | 2 |
Total formula weight | 54048.86 |
Authors | Meir, A.,Waksman, G. (deposition date: 2017-11-07, release date: 2018-02-14, Last modification date: 2024-11-06) |
Primary citation | Meir, A.,Chetrit, D.,Liu, L.,Roy, C.R.,Waksman, G. Legionella DotM structure reveals a role in effector recruiting to the Type 4B secretion system. Nat Commun, 9:507-507, 2018 Cited by PubMed Abstract: 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. PubMed: 29410427DOI: 10.1038/s41467-017-02578-x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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