1d8j: Difference between revisions
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<StructureSection load='1d8j' size='340' side='right'caption='[[1d8j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1d8j' size='340' side='right'caption='[[1d8j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1d8j]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8J FirstGlance]. <br> | <table><tr><td colspan='2'>[[1d8j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8J FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d8k|1d8k]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d8k|1d8k]]</div></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=1d8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8j OCA], [https://pdbe.org/1d8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8j RCSB], [https://www.ebi.ac.uk/pdbsum/1d8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8j ProSAT], [https://www.topsan.org/Proteins/RSGI/1d8j TOPSAN]</span></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=1d8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8j OCA], [https://pdbe.org/1d8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8j RCSB], [https://www.ebi.ac.uk/pdbsum/1d8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8j ProSAT], [https://www.topsan.org/Proteins/RSGI/1d8j TOPSAN]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hanaoka, F]] | [[Category: Hanaoka, F]] | ||
Revision as of 13:36, 16 February 2022
SOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETASOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETA
Structural highlights
Function[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 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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