6FQL

Crystal structure of Danio rerio Lin41 filamin-NHL domains in complex with mab-10 3'UTR 13mer RNA

Summary for 6FQL

• Entry DOI: 10.2210/pdb6fql/pdb
• Related: 6FPT 6FQ3
• Descriptor: E3 ubiquitin-protein ligase TRIM71, RNA (5'-R(*UP*GP*CP*AP*UP*UP*UP*AP*AP*UP*GP*CP*A)-3'), CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: post-transcriptional regulation, rna binding protein
• Biological source: Danio rerio (Zebrafish); More
• Cellular location: Cytoplasm, P-body : E7FAM5
• Total number of polymer chains: 2
• Total formula weight: 49011.91

Authors

Kumari, P.,Aeschimann, F.,Gaidatzis, D.,Keusch, J.J.,Ghosh, P.,Neagu, A.,Pachulska-Wieczorek, K.,Bujnicki, J.M.,Gut, H.,Grosshans, H.,Ciosk, R. (deposition date: 2018-02-14, release date: 2018-05-09, Last modification date: 2024-01-17)

Primary citation

Kumari, P.,Aeschimann, F.,Gaidatzis, D.,Keusch, J.J.,Ghosh, P.,Neagu, A.,Pachulska-Wieczorek, K.,Bujnicki, J.M.,Gut, H.,Grosshans, H.,Ciosk, R.
Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition.
Nat Commun, 9:1549-1549, 2018

PubMed Abstract: RNA-binding proteins regulate all aspects of RNA metabolism. Their association with RNA is mediated by RNA-binding domains, of which many remain uncharacterized. A recently reported example is the NHL domain, found in prominent regulators of cellular plasticity like the C. elegans LIN-41. Here we employ an integrative approach to dissect the RNA specificity of LIN-41. Using computational analysis, structural biology, and in vivo studies in worms and human cells, we find that a positively charged pocket, specific to the NHL domain of LIN-41 and its homologs (collectively LIN41), recognizes a stem-loop RNA element, whose shape determines the binding specificity. Surprisingly, the mechanism of RNA recognition by LIN41 is drastically different from that of its more distant relative, the fly Brat. Our phylogenetic analysis suggests that this reflects a rapid evolution of the domain, presenting an interesting example of a conserved protein fold that acquired completely different solutions to RNA recognition.

PubMed: 29674686
DOI: 10.1038/s41467-018-03920-7

Experimental method

X-RAY DIFFRACTION (2.349 Å)