ArticleScientific reports2022
Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The association of the rumen virome with methane emissions in dairy cattle.Communications biology · 2025Article
- Intra species dissection of phytophthora capsici resistance in black pepper.Journal of advanced research · 2025Article
- Endogenous virophages are active and mitigate giant virus infection in the marine protistProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multi-stage nuclear transcriptomic insights of morphogenesis and biparental role changes in Lentinula edodes.Applied microbiology and biotechnology · 2023Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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