5VRQ

Crystal structure of Legionella pneumophila effector AnkC

Summary for 5VRQ

• Entry DOI: 10.2210/pdb5vrq/pdb
• Descriptor: Ankyrin repeat-containing protein (2 entities in total)
• Functional Keywords: bacterial effector, ankyrin repeats, legionella, protein binding, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi
• Biological source: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• Total number of polymer chains: 1
• Total formula weight: 45743.21

Authors

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) (deposition date: 2017-05-11, release date: 2017-11-29, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.205 Å)