1d8k: Difference between revisions
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==SOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETA== | |||
<StructureSection load='1d8k' size='340' side='right'caption='[[1d8k]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1d8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8K FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1d8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8k OCA], [https://pdbe.org/1d8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8k RCSB], [https://www.ebi.ac.uk/pdbsum/1d8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8k ProSAT], [https://www.topsan.org/Proteins/RSGI/1d8k TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/T2EB_HUMAN T2EB_HUMAN] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. | |||
== 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/d8/1d8k_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=1d8k ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human general transcription factor TFIIE consists of two subunits, TFIIEalpha and TFIIEbeta. Recently, TFIIEbeta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. Here, the central core domain of human TFIIEbeta (TFIIEbetac) has been identified by a limited proteolysis. This solution structure has been determined by NMR. It consists of three helices with a beta hairpin at the C-terminus, resembling the winged helix proteins. However, TFIIEbetac shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow. A model will be proposed that TFIIE stabilizes the preinitiation complex by binding not only to the general transcription factors together with RNA polymerase II but also to the promoter DNA, where double-stranded DNA starts to open to be single-stranded upon activation of the preinitiation complex. | |||
Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.,Okuda M, Watanabe Y, Okamura H, Hanaoka F, Ohkuma Y, Nishimura Y EMBO J. 2000 Mar 15;19(6):1346-56. PMID:10716934<ref>PMID:10716934</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1d8k" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hanaoka | [[Category: Large Structures]] | ||
[[Category: Nishimura | [[Category: Hanaoka F]] | ||
[[Category: Ohkuma | [[Category: Nishimura Y]] | ||
[[Category: Okamura | [[Category: Ohkuma Y]] | ||
[[Category: Okuda | [[Category: Okamura H]] | ||
[[Category: Okuda M]] | |||
[[Category: Watanabe | [[Category: Watanabe Y]] | ||
Latest revision as of 11:23, 22 May 2024
SOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETASOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETA
Structural highlights
FunctionT2EB_HUMAN Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman general transcription factor TFIIE consists of two subunits, TFIIEalpha and TFIIEbeta. Recently, TFIIEbeta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. Here, the central core domain of human TFIIEbeta (TFIIEbetac) has been identified by a limited proteolysis. This solution structure has been determined by NMR. It consists of three helices with a beta hairpin at the C-terminus, resembling the winged helix proteins. However, TFIIEbetac shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow. A model will be proposed that TFIIE stabilizes the preinitiation complex by binding not only to the general transcription factors together with RNA polymerase II but also to the promoter DNA, where double-stranded DNA starts to open to be single-stranded upon activation of the preinitiation complex. Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.,Okuda M, Watanabe Y, Okamura H, Hanaoka F, Ohkuma Y, Nishimura Y EMBO J. 2000 Mar 15;19(6):1346-56. PMID:10716934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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