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Journal Article

Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins

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Huyton,  Trevor
Department of Cellular Logistics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Jaiswal,  Mamta
Department of Cellular Logistics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Görlich,  Dirk
Department of Cellular Logistics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Citation

Huyton, T., Jaiswal, M., Taxer, W., Fischer, M., & Görlich, D. (2022). Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins. Scientific Reports, 12: 16430. doi:10.1038/s41598-022-20758-8.


Cite as: https://hdl.handle.net/21.11116/0000-000C-6CEF-F
Abstract
The Cafeteria roenbergensis virus (Crov), Dictyostelium, and other species encode a large family of leucine-rich repeat (LRR) proteins with FGxxFN motifs. We determined the structures of two of them and observed several unique structural features that set them aside from previously characterized LRR family members. Crov588 comprises 25 regular repeats with a LxxLxFGxxFNQxIxENVLPxx consensus, forming a unique closed circular repeat structure. Novel features include a repositioning of a conserved asparagine at the middle of the repeat, a double phenylalanine spine that generates an alternate core packing arrangement, and a histidine/tyrosine ladder on the concave surface. Crov539 is smaller, comprising 12 repeats of a similar LxxLxFGxxFNQPIExVxW/LPxx consensus and forming an unusual cap-swapped dimer structure. The phenylalanine spine of Crov539 is supplemented with a tryptophan spine, while a hydrophobic isoleucine-rich patch is found on the central concave surface. We present a detailed analysis of the structures of Crov588 and Crov539 and compare them to related repeat proteins and other LRR classes.