9ff7 | pdb_00009ff7

Structure of the BMOE-crosslinked transcription termination factor Rho in the presence of ppGpp; S84C/M405C double mutant

spinqualitylabelsall models 9ff7, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ff7 is a 12 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.4Å Ligands: ME7, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RHO_ECO57 Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. Publication Abstract from PubMed Bacterial RNA helicase rho is a genome sentinel that terminates the synthesis of damaged and junk RNAs that are not translated by the ribosome. It is unclear how rho is regulated during dormancy or stress, when translation is inefficient and RNAs are vulnerable to rho-mediated release. We use cryogenic electron microscopy, biochemical, and genetic approaches to show that substitutions of residues in the connector between two rho domains or ADP promote the formation of extended Escherichia coli rho filaments. By contrast, (p)ppGpp induces the formation of transient rho dodecamers. Our results demonstrate that ADP and (p)ppGpp nucleotides bound at subunit interfaces inhibit rho ring closure that underpins the hexamer activation, thus favoring the assembly of inactive higher-order oligomers. Connector substitutions and antibiotics that inhibit RNA and protein syntheses trigger rho aggregation in the cell. These and other recent data implicate aggregation as a widespread strategy to tune rho activity. Nucleotide-induced hyper-oligomerization inactivates transcription termination factor rho.,Wang B, Said N, Hilal T, Finazzo M, Wahl MC, Artsimovitch I Nat Commun. 2025 Feb 15;16(1):1653. doi: 10.1038/s41467-025-56824-8. PMID:39952913 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA