1a62: Difference between revisions

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[[Image:1a62.gif|left|200px]]
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{{STRUCTURE_1a62|  PDB=1a62  |  SCENE=  }}  
{{STRUCTURE_1a62|  PDB=1a62  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_9586995}}


==About this Structure==
==About this Structure==
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[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transcription termination]]
[[Category: Transcription termination]]
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Revision as of 13:12, 30 June 2008

File:1a62.png

Template:STRUCTURE 1a62

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

Template:ABSTRACT PUBMED 9586995

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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