2a8v: Difference between revisions

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{{STRUCTURE_2a8v|  PDB=2a8v  |  SCENE=  }}  
{{STRUCTURE_2a8v|  PDB=2a8v  |  SCENE=  }}  


'''RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX'''
===RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Rho]]
[[Category: Rho]]
[[Category: Single-stranded nucleic acid binding domain]]
[[Category: Single-stranded nucleic acid binding domain]]
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Revision as of 15:09, 27 July 2008

File:2a8v.png

Template:STRUCTURE 2a8v

RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEXRHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX

Template:ABSTRACT PUBMED 10230401

About this StructureAbout this Structure

2A8V is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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