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6EXD

Crystal structure of DotM cytoplasmic domain (residues 153-380) SeMet derivative

Summary for 6EXD
Entry DOI10.2210/pdb6exd/pdb
DescriptorIcmP (DotM) (2 entities in total)
Functional Keywordsmembrane protein, secretion system, type 4 secretion system, legionella pneumophila, protein binding
Biological sourceLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Total number of polymer chains2
Total formula weight54048.86
Authors
Meir, A.,Waksman, G. (deposition date: 2017-11-07, release date: 2018-02-14, Last modification date: 2024-11-06)
Primary citationMeir, 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: 29410427
DOI: 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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数据于2025-06-25公开中

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