PMID:9586995
| Citation |
Allison, TJ, Wood, TC, Briercheck, DM, Rastinejad, F, Richardson, JP and Rule, GS (1998) Crystal structure of the RNA-binding domain from transcription termination factor rho. Nat. Struct. Biol. 5:352-6 |
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| Abstract |
Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho. |
| Links | |
| Keywords |
Crystallography, X-Ray; Escherichia coli/chemistry; Models, Molecular; Protein Folding; Protein Structure, Tertiary; Proton-Translocating ATPases/chemistry; RNA-Binding Proteins/chemistry; Rho Factor/chemistry |
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