1pvo
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1pvo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvo, resolution 3.00Å" /> '''X-ray crystal struct...) |
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| - | [[Image:1pvo.gif|left|200px]]<br /><applet load="1pvo" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1pvo, resolution 3.00Å" /> | ||
| - | '''X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP'''<br /> | ||
| - | == | + | ==X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP== |
| - | In bacteria, one of the major transcriptional termination mechanisms | + | <StructureSection load='1pvo' size='340' side='right'caption='[[1pvo]], [[Resolution|resolution]] 3.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1pvo]] 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=1PVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PVO 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]] 3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></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=1pvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvo OCA], [https://pdbe.org/1pvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pvo RCSB], [https://www.ebi.ac.uk/pdbsum/1pvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvo 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/1pvo_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=1pvo 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. | ||
| - | + | 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1pvo" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Helicase 3D structures|Helicase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Berger JM]] | ||
| + | [[Category: Skordalakes E]] | ||
Current revision
X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP
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