2A8V

RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX

Summary for 2A8V

• Entry DOI: 10.2210/pdb2a8v/pdb
• Descriptor: 5'-R(P*CP*CP*C)-3', 5'-R(P*CP*CP*CP*CP*CP*C)-3', RNA BINDING DOMAIN OF RHO TRANSCRIPTION TERMINATION FACTOR, ... (4 entities in total)
• Functional Keywords: rho, ob fold, single-stranded nucleic acid binding domain, protein-rna complex, protein/rna
• Biological source: Escherichia coli
• Total number of polymer chains: 5
• Total formula weight: 42310.84

Authors

Bogden, C.E.,Fass, D.,Bergman, N.,Nichols, M.D.,Berger, J.M. (deposition date: 1998-11-08, release date: 1999-04-26, Last modification date: 2023-08-23)

Primary citation

Bogden, C.E.,Fass, D.,Bergman, N.,Nichols, M.D.,Berger, J.M.
The structural basis for terminator recognition by the Rho transcription termination factor.
Mol.Cell, 3:487-493, 1999

PubMed Abstract: The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer.

PubMed: 10230401
DOI: 10.1016/S1097-2765(00)80476-1

Experimental method

X-RAY DIFFRACTION (2.4 Å)