1pv4: Difference between revisions

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{{Seed}}
[[Image:1pv4.png|left|200px]]


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==X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA==
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<StructureSection load='1pv4' size='340' side='right'caption='[[1pv4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1pv4]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PV4 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_1pv4|  PDB=1pv4  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pv4 OCA], [https://pdbe.org/1pv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pv4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pv4 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/pv/1pv4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1pv4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 A resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites--a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding--point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 A) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.


===X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA===
Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading.,Skordalakes E, Berger JM Cell. 2003 Jul 11;114(1):135-46. PMID:12859904<ref>PMID:12859904</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pv4" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12859904}}, adds the Publication Abstract to the page
*[[Helicase 3D structures|Helicase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12859904 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12859904}}
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</StructureSection>
==About this Structure==
1PV4 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=1PV4 OCA].
 
==Reference==
Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading., Skordalakes E, Berger JM, Cell. 2003 Jul 11;114(1):135-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12859904 12859904]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berger, J M.]]
[[Category: Berger JM]]
[[Category: Skordalakes, E.]]
[[Category: Skordalakes E]]
[[Category: Protein-ssdna complex]]
 
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Retrieved from "https://proteopedia.org/1pv4"