Ankyrin repeats as a dimerization module

Journal Article · Mon Jan 15 04:00:00 EST 2018 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/J.BBRC.2017.11.135· OSTI ID:23134468

Kozlov, Guennadi; Wong, Kathy; Wang, Wenxuan ^[1]; Skubák, Pavol ^[2]; Muñoz-Escobar, Juliana; Liu, Yue ^[1]; Siddiqui, Nadeem ^[3]; Pannu, Navraj S. ^[2]; Gehring, Kalle ^[1]

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1. Department of Biochemistry, Groupe de recherche axé sur la structure des protéines, McGill University, Montreal, QC H3G 0B1 (Canada)
2. Biophysical Structural Chemistry, Leiden University, 2300 RA Leiden (Netherlands)
3. Department of Biochemistry, Goodman Cancer Research Centre, McGill University, Montreal, QC H3A 1A3 (Canada)

Highlights: • 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. 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.

• OSTI ID: 23134468
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 495; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
LEGIONELLA PNEUMOPHILA
PNEUMONIA
PROTEINS