2a8v
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(New page: 200px<br /><applet load="2a8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a8v, resolution 2.4Å" /> '''RHO TRANSCRIPTION TER...)
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Revision as of 05:52, 21 November 2007
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RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX
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
2A8V is a Single protein structure of sequence from Escherichia coli. 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
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