2eul

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(New page: 200px<br /><applet load="2eul" size="350" color="white" frame="true" align="right" spinBox="true" caption="2eul, resolution 2.40&Aring;" /> '''Structure of the tra...)
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[[Image:2eul.gif|left|200px]]<br /><applet load="2eul" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2eul, resolution 2.40&Aring;" />
 
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'''Structure of the transcription factor Gfh1.'''<br />
 
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==Overview==
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==Structure of the transcription factor Gfh1.==
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Gre factors enhance the intrinsic endonucleolytic activity of RNA, polymerase to rescue arrested transcription complexes and are thought to, confer the high fidelity and processivity of RNA synthesis. The Gre, factors insert the extended alpha-helical coiled-coil domains into the RNA, polymerase secondary channel to position two invariant acidic residues at, the coiled-coil tip near the active site to stabilize the catalytic metal, ion. Gfh1, a GreA homolog from Thermus thermophilus, inhibits rather than, activates RNA cleavage. Here we report the structure of the T., thermophilus Gfh1 at 2.4 A resolution revealing a two-domain architecture, closely resembling that of GreA. However, the interdomain orientation is, strikingly distinct (approximately 162 degrees rotation) between the two, proteins. In contrast to GreA, which has two acidic residues on a well, fixed self-stabilized alpha-turn, the tip of the Gfh1 coiled-coil is, flexible and contains four acidic residues. This difference is likely the, key to the Gre functional diversity, while Gfh1 inhibits exo- and, endonucleolytic cleavage, RNA synthesis, and pyrophosphorolysis, GreA, enhances only the endonucleolytic cleavage. We propose that Gfh1 acidic, residues stabilize the RNA polymerase active center in a catalytically, inactive configuration through Mg2+-mediated interactions. The excess of, the acidic residues and inherent flexibility of the coiled-coil tip might, allow Gfh1 to adjust its activity to structurally distinct substrates, thereby inhibiting diverse catalytic reactions of RNA polymerase.
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<StructureSection load='2eul' size='340' side='right'caption='[[2eul]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2eul]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EUL FirstGlance]. <br>
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2EUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUL OCA].
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eul OCA], [https://pdbe.org/2eul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eul RCSB], [https://www.ebi.ac.uk/pdbsum/2eul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eul ProSAT], [https://www.topsan.org/Proteins/RSGI/2eul TOPSAN]</span></td></tr>
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Regulation through the RNA polymerase secondary channel. Structural and functional variability of the coiled-coil transcription factors., Symersky J, Perederina A, Vassylyeva MN, Svetlov V, Artsimovitch I, Vassylyev DG, J Biol Chem. 2006 Jan 20;281(3):1309-12. Epub 2005 Nov 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16298991 16298991]
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</table>
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[[Category: Single protein]]
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== Function ==
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[[Category: Thermus thermophilus]]
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[https://www.uniprot.org/uniprot/GFH1_THET8 GFH1_THET8] Inhibits all catalytic activities of RNA polymerase (RNAP) by partially occluding its substrate-binding site and preventing NTP binding.<ref>PMID:11606592</ref> <ref>PMID:14712703</ref> <ref>PMID:16298991</ref>
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[[Category: Artsimovitch, I.]]
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== Evolutionary Conservation ==
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[[Category: Perederina, A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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Check<jmol>
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[[Category: Svetlov, V.]]
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<jmolCheckbox>
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[[Category: Symersky, J.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eu/2eul_consurf.spt"</scriptWhenChecked>
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[[Category: Vassylyev, D.G.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Vassylyeva, M.N.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: ZN]]
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</jmolCheckbox>
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[[Category: gfh1]]
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</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=2eul ConSurf].
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[[Category: riken structural genomics/proteomics initiative]]
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<div style="clear:both"></div>
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[[Category: rna polymerase]]
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== References ==
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[[Category: rsgi]]
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<references/>
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[[Category: structural genomics]]
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__TOC__
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[[Category: transcription factor]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:21:31 2008''
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[[Category: Thermus thermophilus HB8]]
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[[Category: Artsimovitch I]]
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[[Category: Perederina A]]
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[[Category: Svetlov V]]
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[[Category: Symersky J]]
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[[Category: Vassylyev DG]]
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[[Category: Vassylyeva MN]]

Current revision

Structure of the transcription factor Gfh1.

PDB ID 2eul

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