1a62: Difference between revisions
New page: left|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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[[Image:1a62.gif|left|200px]]<br /><applet load="1a62" size=" | [[Image:1a62.gif|left|200px]]<br /><applet load="1a62" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1a62, resolution 1.55Å" /> | caption="1a62, resolution 1.55Å" /> | ||
'''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO'''<br /> | '''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO'''<br /> | ||
==Overview== | ==Overview== | ||
Transcription termination factor rho is an ATP-dependent hexameric | 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== | ==About this Structure== | ||
1A62 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1A62 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Allison, T | [[Category: Allison, T J.]] | ||
[[Category: Briercheck, D | [[Category: Briercheck, D M.]] | ||
[[Category: Rastinejad, F.]] | [[Category: Rastinejad, F.]] | ||
[[Category: Richardson, J | [[Category: Richardson, J P.]] | ||
[[Category: Rule, G | [[Category: Rule, G S.]] | ||
[[Category: Wood, T | [[Category: Wood, T C.]] | ||
[[Category: f1-atpase]] | [[Category: f1-atpase]] | ||
[[Category: ob fold]] | [[Category: ob fold]] | ||
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[[Category: transcription termination]] | [[Category: transcription termination]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:15 2008'' | ||
Revision as of 09:41, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 11:41:15 2008
