Ankyrin repeats as a dimerization module

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2018-01, Vol.495 (1), p.1002-1007
Main Authors: Kozlov, Guennadi, Wong, Kathy, Wang, Wenxuan, Skubák, Pavol, Muñoz-Escobar, Juliana, Liu, Yue, Siddiqui, Nadeem, Pannu, Navraj S., Gehring, Kalle
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Ankyrin Repeat
Ankyrins - chemistry
Ankyrins - ultrastructure
Binding Sites
Computer Simulation
Conserved Sequence
LegA12
Legionella pneumophila - metabolism
lpg0483
Models, Chemical
Models, Molecular
Molecular Sequence Data
Pathogen
Protein Binding
Protein Conformation
Protein Multimerization
Virulence factor
X-ray crystallography
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Summary: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. •We determined crystal structure of Legionella effector AnkC.•The structure displays seven ankyrin repeats with unique structural features.•AnkC dimerizes using outer surface of loops between ankyrin repeats.•This is the first example of ankyrin repeats-mediated dimerization.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2017.11.135