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[[Image:2a8v.gif|left|200px]]
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{{STRUCTURE_2a8v|  PDB=2a8v  |  SCENE=  }}
'''RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX'''


==RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX==
<StructureSection load='2a8v' size='340' side='right'caption='[[2a8v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a8v]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A8V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8v OCA], [https://pdbe.org/2a8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a8v RCSB], [https://www.ebi.ac.uk/pdbsum/2a8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RHO_ECOLI RHO_ECOLI] Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/2a8v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a8v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:10230401</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 2a8v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Escherichia coli K-12]]
[[Category: Berger, J M.]]
[[Category: Large Structures]]
[[Category: Bergman, N.]]
[[Category: Berger JM]]
[[Category: Bogden, C E.]]
[[Category: Bergman N]]
[[Category: Fass, D.]]
[[Category: Bogden CE]]
[[Category: Nichols, M D.]]
[[Category: Fass D]]
[[Category: Ob fold]]
[[Category: Nichols MD]]
[[Category: Protein/rna complex]]
[[Category: Rho]]
[[Category: Single-stranded nucleic acid binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:45:25 2008''
Retrieved from "https://proteopedia.org/2a8v"