8bvm

Cryo-EM structure of Hfq-Crc-rbsB translation repression complexCryo-EM structure of Hfq-Crc-rbsB translation repression complex

Structural highlights 8bvm is a 16 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q51380_PSEAI Publication Abstract from PubMed The widely occurring bacterial RNA chaperone Hfq is a key factor in the post-transcriptional control of hundreds of genes in Pseudomonas aeruginosa. How this broadly acting protein can contribute to the regulatory requirements of many different genes remains puzzling. Here, we describe cryo-EM structures of higher order assemblies formed by Hfq and its partner protein Crc on control regions of different P. aeruginosa target mRNAs. Our results show that these assemblies have mRNA-specific quaternary architectures resulting from the combination of multivalent protein-protein interfaces and recognition of patterns in the RNA sequence. The structural polymorphism of these ribonucleoprotein assemblies enables selective translational repression of many different target mRNAs. This system elucidates how highly complex regulatory pathways can evolve with a minimal economy of proteinogenic components in combination with RNA sequence and fold. Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.,Dendooven T, Sonnleitner E, Blasi U, Luisi BF EMBO J. 2023 Feb 1;42(3):e111129. doi: 10.15252/embj.2022111129. Epub 2022 Dec , 12. PMID:36504222 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein Hfq 3D structures

spinqualitylabelsall models 8bvm, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image