2a8v
From Proteopedia
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| - | [[Image:2a8v.gif|left|200px]] | + | [[Image:2a8v.gif|left|200px]] |
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| - | '''RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX''' | + | {{Structure |
| + | |PDB= 2a8v |SIZE=350|CAPTION= <scene name='initialview01'>2a8v</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A8V is a [ | + | 2A8V is a [[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=2A8V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10230401 10230401] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: single-stranded nucleic acid binding domain]] | [[Category: single-stranded nucleic acid binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:47 2008'' |
Revision as of 13:46, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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