1a8v
From Proteopedia
(New page: 200px<br /><applet load="1a8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a8v, resolution 2.0Å" /> '''STRUCTURE OF THE RNA-...) |
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| - | [[Image:1a8v.jpg|left|200px]]<br /><applet load="1a8v" size=" | + | [[Image:1a8v.jpg|left|200px]]<br /><applet load="1a8v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a8v, resolution 2.0Å" /> | caption="1a8v, resolution 2.0Å" /> | ||
'''STRUCTURE OF THE RNA-BINDING DOMAIN OF THE RHO TRANSCRIPTION TERMINATOR'''<br /> | '''STRUCTURE OF THE RNA-BINDING DOMAIN OF THE RHO TRANSCRIPTION TERMINATOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The E. coli Rho protein disengages newly transcribed RNA from its DNA | + | The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer. |
==About this Structure== | ==About this Structure== | ||
| - | 1A8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1A8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Berger, J | + | [[Category: Berger, J M.]] |
[[Category: Bogden, C.]] | [[Category: Bogden, C.]] | ||
[[Category: Fass, D.]] | [[Category: Fass, D.]] | ||
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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 11:42:14 2008'' |
Revision as of 09:42, 21 February 2008
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STRUCTURE OF THE RNA-BINDING DOMAIN OF THE RHO TRANSCRIPTION TERMINATOR
Overview
The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer.
About this Structure
1A8V is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
The structural basis for terminator recognition by the Rho transcription termination factor., Bogden CE, Fass D, Bergman N, Nichols MD, Berger JM, Mol Cell. 1999 Apr;3(4):487-93. PMID:10230401
Page seeded by OCA on Thu Feb 21 11:42:14 2008
