1PV4

X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA

Summary for 1PV4

• Entry DOI: 10.2210/pdb1pv4/pdb
• Related: 1PVO
• Descriptor: 5'-D(P*CP*C)-3', Transcription termination factor rho (3 entities in total)
• Functional Keywords: protein-ssdna complex, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 11
• Total formula weight: 289589.91

Authors

Skordalakes, E.,Berger, J.M. (deposition date: 2003-06-26, release date: 2003-07-22, Last modification date: 2024-10-09)

Primary citation

Skordalakes, E.,Berger, J.M.
Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
Cell(Cambridge,Mass.), 114:135-146, 2003

PubMed Abstract: In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 A resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites--a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding--point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 A) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.

PubMed: 12859904
DOI: 10.1016/S0092-8674(03)00512-9

Experimental method

X-RAY DIFFRACTION (3 Å)