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6O1M

Architectural principles for Hfq/Crc-mediated regulation of gene expression. Hfq-Crc-amiE 2:4:2 complex

Summary for 6O1M
Entry DOI10.2210/pdb6o1m/pdb
EMDB information0592
DescriptorCatabolite repression control protein, RNA-binding protein Hfq, RNA (5'-R(*AP*AP*AP*AP*AP*UP*AP*AP*CP*AP*AP*CP*AP*AP*GP*AP*GP*G)-3') (3 entities in total)
Functional Keywordshfq, crc, amie, carbon catabolite repression, rna-protein interaction, rna-mediated gene regulation, rna binding protein, rna binding protein-rna-hydrolase complex, rna binding protein/rna/hydrolase
Biological sourcePseudomonas aeruginosa
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Total number of polymer chains18
Total formula weight224354.60
Authors
Pei, X.Y.,Dendooven, T.,Sonnleitner, E.,Chen, S.,Blasi, U.,Luisi, B.F. (deposition date: 2019-02-20, release date: 2019-03-13, Last modification date: 2024-03-20)
Primary citationPei, X.Y.,Dendooven, T.,Sonnleitner, E.,Chen, S.,Blasi, U.,Luisi, B.F.
Architectural principles for Hfq/Crc-mediated regulation of gene expression.
Elife, 8:-, 2019
Cited by
PubMed Abstract: In diverse bacterial species, the global regulator Hfq contributes to post-transcriptional networks that control expression of numerous genes. Hfq of the opportunistic pathogen inhibits translation of target transcripts by forming a regulatory complex with the catabolite repression protein Crc. This repressive complex acts as part of an intricate mechanism of preferred nutrient utilisation. We describe high-resolution cryo-EM structures of the assembly of Hfq and Crc bound to the translation initiation site of a target mRNA. The core of the assembly is formed through interactions of two cognate RNAs, two Hfq hexamers and a Crc pair. Additional Crc protomers are recruited to the core to generate higher-order assemblies with demonstrated regulatory activity in vivo. This study reveals how Hfq cooperates with a partner protein to regulate translation, and provides a structural basis for an RNA code that guides global regulators to interact cooperatively and regulate different RNA targets.
PubMed: 30758287
DOI: 10.7554/eLife.43158
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.15 Å)
Structure validation

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