Crystal structure of the RNA-binding domain from transcription termination factor rho.
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.
Allison
T J
TJ
Wood
T C
TC
Briercheck
D M
DM
Rastinejad
F
F
Richardson
J P
JP
Rule
G S
GS
D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry*; D012234:Rho Factor / Q000737:chemistry*
D016601:RNA-Binding Proteins; D012234:Rho Factor; D006180:Proton-Translocating ATPases