6EXD

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

6EXD の概要

• エントリーDOI: 10.2210/pdb6exd/pdb
• 分子名称: IcmP (DotM) (2 entities in total)
• 機能のキーワード: membrane protein, secretion system, type 4 secretion system, legionella pneumophila, protein binding
• 由来する生物種: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54048.86

構造登録者

Meir, A.,Waksman, G. (登録日: 2017-11-07, 公開日: 2018-02-14, 最終更新日: 2024-11-06)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.14 Å)