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. 2019 Jul 23;9:10675. doi: 10.1038/s41598-019-47034-6

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Schematic and structural representation of PfK13 and its putative function as substrate adaptor. (a) PfK13 domain annotation. Three domains of PfK13 are annotated in databases: coiled-coil-containing (CCC), BTB, and Kelch-repeat propeller (KREP). The Apicomplexa-specific N-terminal domain is predicted to exhibit a random-coil conformation. The crystal structure of BTB and KREP domains was solved; the CCC domain is expected to form two helices coiling together. (b) Proposed, simplified model of the protein complex containing PfK13, based on PfK13 domain annotation and co-immunoprecipitation experiments^{17,21,22,89,90}. The BTB domain of PfK13 is expected to bind a scaffold Cullin protein, while the KREP domain likely binds to the substrate molecule(s) further ubiquitinated and possibly degraded by the proteasome. Importantly, the regions and sites of PfK13 involved in binding are unknown (represented as red ‘?’ symbol in the figure). For ease of representation, PfK13 was shown as a monomer although the crystal structure of PfK13 BTB-KREP was solved as a dimer.