3FXE

Crystal structure of interacting domains of IcmR and IcmQ (seleno-derivative)

3FXE の概要

• エントリーDOI: 10.2210/pdb3fxe/pdb
• 分子名称: Protein IcmQ, Protein IcmR (3 entities in total)
• 機能のキーワード: 4 helix bundle, helix-turn-helix, se-met, unknown function
• 由来する生物種: Legionella pneumophila; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14417.19

構造登録者

Raychaudhury, S.,Akey, C.W.,Head, J.F. (登録日: 2009-01-20, 公開日: 2009-04-28, 最終更新日: 2024-11-06)

主引用文献

Raychaudhury, S.,Farelli, J.D.,Montminy, T.P.,Matthews, M.,Menetret, J.F.,Dumenil, G.,Roy, C.R.,Head, J.F.,Isberg, R.R.,Akey, C.W.
Structure and Function of Interacting IcmR-IcmQ Domains from a Type IVb Secretion System in Legionella pneumophila.
Structure, 17:590-601, 2009

PubMed Abstract: During infection, Legionella pneumophila creates a replication vacuole within eukaryotic cells and this requires a Type IVb secretion system (T4bSS). IcmQ plays a critical role in the translocase and associates with IcmR. In this paper, we show that the N-terminal domain of IcmQ (Qn) mediates self-dimerization, whereas the C-terminal domain with a basic linker promotes membrane association. In addition, the binding of IcmR to IcmQ prevents self-dimerization and also blocks membrane permeabilization. However, IcmR does not completely block membrane binding by IcmQ. We then determined crystal structures of Qn with the interacting region of IcmR. In this complex, each protein forms an alpha-helical hairpin within a parallel four-helix bundle. The amphipathic nature of helices in Qn suggests two possible models for membrane permeabilization by IcmQ. The Rm-Qn structure also suggests how IcmR-like proteins in other L. pneumophila species may interact with their IcmQ partners.

PubMed: 19368892
DOI: 10.1016/j.str.2009.02.011

実験手法

X-RAY DIFFRACTION (2.2 Å)