7BYK

Crystal structure of the Legionella pneumophila LegK7 effector kinase

7BYK の概要

• エントリーDOI: 10.2210/pdb7byk/pdb
• 分子名称: LegK7 (2 entities in total)
• 機能のキーワード: protein kinase, legionella pneumophila, transferase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 110798.32

構造登録者

Park, S.C.,Kim, T.H.,Yoon, S.I. (登録日: 2020-04-23, 公開日: 2020-12-30, 最終更新日: 2024-03-27)

主引用文献

Park, S.C.,Cho, S.Y.,Kim, T.H.,Ko, K.Y.,Song, W.S.,Kang, S.G.,Lee, G.S.,Yoon, S.I.
Activation of the Legionella pneumophila LegK7 Effector Kinase by the Host MOB1 Protein.
J.Mol.Biol., 433:166746-166746, 2020

PubMed Abstract: Legionella pneumophila infects alveolar macrophages and can cause life-threatening pneumonia in humans. Upon internalization into the host cell, L. pneumophila injects numerous effector proteins into the host cytoplasm as a part of its pathogenesis. LegK7 is an effector kinase of L. pneumophila that functionally mimics the eukaryotic Mst kinase and phosphorylates the host MOB1 protein to exploit the Hippo pathway. To elucidate the LegK7 activation mechanism, we determined the apo structure of LegK7 in an inactive form and performed a comparative analysis of LegK7 structures. LegK7 is a non-RD kinase that contains an activation segment that is ordered, irrespective of stimulation, through a unique β-hairpin-containing segment, and it does not require phosphorylation of the activation segment for activation. Instead, bacterial LegK7 becomes an active kinase via its heterologous molecular interaction with the host MOB1 protein. MOB1 binding triggers reorientation of the two lobes of the kinase domain, as well as a structural change in the interlobe hinge region in LegK7, consequently reshaping the LegK7 structure into an ATP binding-compatible closed conformation. Furthermore, we reveal that LegK7 is an atypical kinase that contains an N-terminal capping domain and a hydrophilic interlobe linker motif, which play key roles in the MOB1-induced activation of LegK7.

PubMed: 33309852
DOI: 10.1016/j.jmb.2020.166746

実験手法

X-RAY DIFFRACTION (2.65 Å)