1A8V

STRUCTURE OF THE RNA-BINDING DOMAIN OF THE RHO TRANSCRIPTION TERMINATOR

Summary for 1A8V

• Entry DOI: 10.2210/pdb1a8v/pdb
• Descriptor: TRANSCRIPTION TERMINATION FACTOR RHO, COPPER (II) ION (3 entities in total)
• Functional Keywords: transcription termination, rna-binding, terminator, rho protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 27215.97

Authors

Fass, D.,Bogden, C.,Berger, J.M. (deposition date: 1998-03-28, release date: 1999-05-04, Last modification date: 2024-02-07)

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 Å)