1A62

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO

Summary for 1A62

• Entry DOI: 10.2210/pdb1a62/pdb
• Descriptor: RHO (2 entities in total)
• Functional Keywords: transcription termination, termination, rna binding domain, transcription regulation, ob fold, f1-atpase
• Biological source: Escherichia coli BL21(DE3)
• Total number of polymer chains: 1
• Total formula weight: 14775.29

Authors

Allison, T.J.,Wood, T.C.,Briercheck, D.M.,Rastinejad, F.,Richardson, J.P.,Rule, G.S. (deposition date: 1998-03-05, release date: 1998-06-17, Last modification date: 2024-10-30)

Primary citation

Allison, T.J.,Wood, T.C.,Briercheck, D.M.,Rastinejad, F.,Richardson, J.P.,Rule, G.S.
Crystal structure of the RNA-binding domain from transcription termination factor rho.
Nat.Struct.Biol., 5:352-356, 1998

PubMed 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.

PubMed: 9586995
DOI: 10.1038/nsb0598-352

Experimental method

X-RAY DIFFRACTION (1.55 Å)