4MU6

Crystal Structure of the N-terminal domain of Effector Protein LegC3 from Legionella pneumophila

4MU6 の概要

• エントリーDOI: 10.2210/pdb4mu6/pdb
• 分子名称: Kinectin 1 (Kinesin receptor) (2 entities in total)
• 機能のキーワード: structural genomics, unknown function
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42789.26

構造登録者

Yao, D.,Cherney, M.,Cygler, M. (登録日: 2013-09-20, 公開日: 2013-12-11, 最終更新日: 2017-11-15)

主引用文献

Yao, D.,Cherney, M.,Cygler, M.
Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila.
Acta Crystallogr.,Sect.D, 70:436-441, 2014

PubMed Abstract: Legionella pneumophila secretes over 300 effectors during the invasion of human cells. The functions of only a small number of them have been identified. LegC3 is one of the identified effectors, which is believed to act by inhibiting vacuolar fusion. It contains two predicted transmembrane helices that divide the protein into a larger N-terminal domain and a smaller C-terminal domain. The function of LegC3 has been shown to be associated primarily with the N-terminal domain, which contains coiled-coil sequence motifs. The structure of the N-terminal domain has been determined and it is shown that it is highly α-helical and contains a helical bundle followed by a long antiparallel coiled-coil. No similar protein fold has been observed in the PDB. A long loop at the tip of the coiled-coil distal from the membrane is disordered and may be important for interaction with an as yet unidentified protein.

PubMed: 24531477
DOI: 10.1107/S139900471302991X

実験手法

X-RAY DIFFRACTION (2.082 Å)