5VRQ

Crystal structure of Legionella pneumophila effector AnkC

5VRQ の概要

• エントリーDOI: 10.2210/pdb5vrq/pdb
• 分子名称: Ankyrin repeat-containing protein (2 entities in total)
• 機能のキーワード: bacterial effector, ankyrin repeats, legionella, protein binding, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi
• 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: 1
• 化学式量合計: 45743.21

構造登録者

Kozlov, G.,Wong, K.,Wang, W.,Skubak, P.,Munoz-Escobar, J.,Liu, Y.,Pannu, N.S.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2017-05-11, 公開日: 2017-11-29, 最終更新日: 2024-03-13)

主引用文献

Kozlov, G.,Wong, K.,Wang, W.,Skubak, P.,Munoz-Escobar, J.,Liu, Y.,Siddiqui, N.,Pannu, N.S.,Gehring, K.
Ankyrin repeats as a dimerization module.
Biochem. Biophys. Res. Commun., 495:1002-1007, 2018

PubMed Abstract: Legionella pneumophila is a pathogen, causing severe pneumonia in humans called Legionnaires' disease. AnkC (LegA12) is a poorly characterized 495-residue effector protein conserved in multiple Legionella species. Here, we report the crystal structure of a C-terminally truncated AnkC (2-384) at 3.2 Å resolution. The structure shows seven ankyrin repeats (ARs) with unique structural features. AnkC forms a dimer along the outer surface of loops between ARs. The dimer exists both in the crystal form and in solution, as shown by analytical ultracentrifugation. This is the first example of ARs as a dimerization module as opposed to solely a protein interaction domain. In addition, a novel α-helix insert between AR3-AR4 is positioned across the surface opposite the ankyrin groove. Sequence conservation suggests that the ankyrin groove of AnkC is a functional site that interacts with binding targets. This ankyrin domain structure is an important step towards a functional characterization of AnkC.

PubMed: 29175332
DOI: 10.1016/j.bbrc.2017.11.135

実験手法

X-RAY DIFFRACTION (3.205 Å)