1a62
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(New page: 200px<br /><applet load="1a62" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a62, resolution 1.55Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 08:30, 20 November 2007
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CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO
Overview
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.
About this Structure
1A62 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the RNA-binding domain from transcription termination factor rho., Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS, Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995
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