5vrq | pdb_00005vrq

Crystal structure of Legionella pneumophila effector AnkC

spinqualitylabelsall models 5vrq, resolution 3.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vrq is a 1 chain structure with sequence from Legph. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: legA12, lpg0483 (LEGPH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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 alpha-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. Ankyrin repeats as a dimerization module.,Kozlov G, Wong K, Wang W, Skubak P, Munoz-Escobar J, Liu Y, Siddiqui N, Pannu NS, Gehring K Biochem Biophys Res Commun. 2017 Nov 21. pii: S0006-291X(17)32314-8. doi:, 10.1016/j.bbrc.2017.11.135. PMID:29175332 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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